2022/05/02 更新

写真a

シャバス レオナルド ミッシェル ガブリエル ヘンリ
CHAVAS Leonard Michel Gabriel Henri
CHAVAS Leonard Michel Gabriel Henri
所属
シンクロトロン光研究センター シンクロトロン光利用研究部門 教授
大学院担当
大学院工学研究科
職名
教授
連絡先
メールアドレス
プロフィール
Frenchy expatriated in Japan, passionate by synchrotron radiation and related methodologies to unravel the mysteries behind biology, loving father of 3
外部リンク

学位 3

  1. 博士(理学) ( 2005年9月   総合研究大学院大学 ) 

  2. M.S. Functional and Structural Biology ( 2002年6月 ) 

  3. B.S. Biochemistry ( 2000年6月 ) 

研究キーワード 8

  1. Biomolecular physics

  2. In vivo crystallography

  3. Synchrotron radiation

  4. Structural biology

  5. Integrated biology

  6. Microfluidic

  7. HPPX

  8. Protein crystallography

研究分野 6

  1. ライフサイエンス / 構造生物化学  / Protein crystallography

  2. ライフサイエンス / 生物物理学

  3. ナノテク・材料 / 生体化学  / in vivo crystallography

  4. ライフサイエンス / 機能生物化学  / Integrated biology

  5. ライフサイエンス / 薬系化学、創薬科学  / Structure-based Drug Design

  6. 情報通信 / 生命、健康、医療情報学  / Multi-scale imaging informatics

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現在の研究課題とSDGs 3

  1. 大規模構造解析施設等を活用したタンパク質等相関構造解析による支援と高度化

  2. Structural studies and modification of glucose dehydrogenases to create enzymatic biofuel cells with enhanced properties

  3. 遺伝子工学を用いたサステナブルフード:生体生産結晶

経歴 8

  1. 名古屋大学   教授

    2021年3月 - 現在

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    国名:日本国

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  2. 名古屋大学   教授

    2021年3月 - 現在

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    国名:日本国

  3. Synchrotron SOLEIL (France)   Health and Biology section   Chief Researcher   Head of Biology Scientific section

    2017年1月 - 2021年2月

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    国名:フランス共和国

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  4. Synchrotron SOLEIL (France)   Beamline PROXIMA-1   Chief Researcher   Beamline manager & Group leader

    2015年6月 - 2021年2月

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    国名:フランス共和国

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  5. DESY (Germany)   Center for Free Electron Laser sciences   Chief Researcher   Scientist & Team leader

    2013年9月 - 2015年5月

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    国名:ドイツ連邦共和国

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  6. 高エネルギー加速器研究機構   助教授

    2009年4月 - 2013年8月

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    国名:日本国

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  7. The University of Manchester (UK)   Department of Life Sciences   Researcher   Research associate

    2007年9月 - 2009年3月

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    国名:グレートブリテン・北アイルランド連合王国(英国)

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  8. High Accelerator Research Organization   Structural Biology Research Center   Researcher   Post-doctoral fellow

    2005年10月 - 2007年

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    国名:日本国

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学歴 3

  1. 総合研究大学院大学

    2002年 - 2005年

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    国名: 日本国

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  2. Joseph Fourier University

    2000年 - 2002年

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    国名: フランス共和国

  3. Joseph Fourier University

    1999年 - 2000年

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    国名: フランス共和国

所属学協会 6

  1. 日本結晶学会   委員

    2021年4月 - 現在

  2. 日本放射光学会   委員

    2021年4月 - 現在

  3. Association Française de Cristallographie   委員

    2015年1月 - 現在

  4. Société Française de Biophysique   委員

    2021年7月 - 現在

  5. 公益社団法人日本生化学会   委員

    2021年4月 - 現在

  6. 一般社団法人日本蛋白質科学会   委員

    2021年4月 - 現在

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委員歴 4

  1. 日本結晶学会   日本結晶学会年次総会2024年組織委員会  

    2022年2月 - 現在   

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    団体区分:学協会

  2. 公益社団法人日本生化学会   第60回日本生物物理学会年会年  

    2022年2月 - 現在   

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    団体区分:学協会

  3. 一般社団法人日本蛋白質科学会   第22回日本蛋白質科学会年会  

    2022年1月 - 現在   

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    団体区分:学協会

  4. シンクロトロン光研究センター   シンクロトロン光研究センター運営委員会  

    2021年4月 - 現在   

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    団体区分:その他

 

論文 61

  1. Implementation of wedged-serial protein crystallography at PROXIMA-1 査読有り 国際共著 国際誌

    Chaussavoine I., Isabet T., Lener R., Montaville P., Vasireddi R., Chavas L.M.G.

    Journal of Synchrotron Radiation   29 巻   頁: 439 - 446   2022年3月

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    記述言語:日本語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Journal of Synchrotron Radiation  

    An approach for serial crystallography experiments based on wedged-data collection is described. This is an alternative method for recording in situ X-ray diffraction data on crystalline samples efficiently loaded in an X-ray compatible microfluidic chip. Proper handling of the microfluidic chip places crystalline samples at geometrically known positions with respect to the focused X-ray interaction area for serial data collection of small wedges. The integration of this strategy takes advantage of the greatly modular sample environment available on the endstation, which allows access to both in situ and more classical cryocrystallography with minimum time loss. The method represents another optional data collection approach that adds up to the already large set of methods made available to users. Coupled with the advances in processing serial crystallography data, the wedged-data collection strategy proves highly efficient in minimizing the amount of required sample crystals for recording a complete dataset. From the advances in microfluidic technology presented here, highthroughput room-temperature crystallography experiments may become routine and should be easily extended to industrial use.

    DOI: 10.1107/S1600577521013242

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  2. Structure of recombinantly expressed cockroach Lili-Mip protein in glycosylated and deglycosylated forms 査読有り 国際共著 国際誌

    KanagaVijayan D., Subramanian R., Santhakumari P.R., Chavas L.M.G., Subramanian R., Banerjee S.

    Biochimica et Biophysica Acta - General Subjects   1866 巻 ( 3 ) 頁: 130064   2022年3月

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    記述言語:日本語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Biochimica et Biophysica Acta - General Subjects  

    Background: The Pacific Beetle Cockroach is the only known viviparous cockroach. The pregnant females provide nutrition to the embryos by secreting milk proteins (Lili-Mips), which crystallize in vivo. The crystals that grow in the embryo are heterogeneous in their protein sequence. It is not apparent from the structure determined what role heterogeneity and glycosylation played in crystallization. Lili-Mips are very nutritious. Methods: Here, we report the cloning of synthesized Lili-Mip genes, their expression in Saccharomyces cerevisiae as secreted proteins, purification, crystallization, and the determination of a three-dimensional structure of one glycosylated and one deglycosylated form. Results: A 2.35 Å structure of the glycosylated form is bound to palmitoleic acid and has several Zn atom mediated interactions. A 1.45 Å structure of the deglycosylated protein revals a binding pocket that has both oleic and palmitoleic acid bound. Mass-spectrometry shows that oleic acid and palmitoleic acid are bound to the protein. Docking studies suggest that aliphatic chains of lengths 15, 16, and 18 carbons bind well in the pocket. Conclusions: The recombinantly expressed and secreted protein is glycosylated, has a bound fatty acid, is homogenous in its protein sequences, and readily forms crystals. The deglycosylated protein also crystallizes readily, suggesting that the high crystallizability of this protein is independent of glycosylation. General significance: Lili-Mips belong to the ubiquitous lipocalin family of proteins that bind to a large variety of ligands. While the residues lining the barrel are essential for the affinity of the ligand, our results show the role of side-chain orientations to ligand selectivity.

    DOI: 10.1016/j.bbagen.2021.130064

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  3. Crystallographic snapshots of a B<inf>12</inf>-dependent radical SAM methyltransferase 査読有り 国際共著 国際誌

    Fyfe C.D., Bernardo-García N., Fradale L., Grimaldi S., Guillot A., Brewee C., Chavas L.M.G., Legrand P., Benjdia A., Berteau O.

    Nature   602 巻 ( 7896 ) 頁: 336 - 342   2022年2月

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    記述言語:日本語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Nature  

    By catalysing the microbial formation of methane, methyl-coenzyme M reductase has a central role in the global levels of this greenhouse gas1,2. The activity of methyl-coenzyme M reductase is profoundly affected by several unique post-translational modifications3–6, such as a unique C-methylation reaction catalysed by methanogenesis marker protein 10 (Mmp10), a radical S-adenosyl-l-methionine (SAM) enzyme7,8. Here we report the spectroscopic investigation and atomic resolution structure of Mmp10 from Methanosarcina acetivorans, a unique B12 (cobalamin)-dependent radical SAM enzyme9. The structure of Mmp10 reveals a unique enzyme architecture with four metallic centres and critical structural features involved in the control of catalysis. In addition, the structure of the enzyme–substrate complex offers a glimpse into a B12-dependent radical SAM enzyme in a precatalytic state. By combining electron paramagnetic resonance spectroscopy, structural biology and biochemistry, our study illuminates the mechanism by which the emerging superfamily of B12-dependent radical SAM enzymes catalyse chemically challenging alkylation reactions and identifies distinctive active site rearrangements to provide a structural rationale for the dual use of the SAM cofactor for radical and nucleophilic chemistry.

    DOI: 10.1038/s41586-021-04355-9

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  4. Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level 査読有り 国際共著 国際誌

    Otero L.H., Foscaldi S., Antelo G.T., Rosano G.L., Sirigu S., Klinke S., Defelipe L.A., Sánchez-Lamas M., Battocchio G., Conforte V., Vojnov A.A., Chavas L.M.G., Goldbaum F.A., Mroginski M.A., Rinaldi J., Bonomi H.R.

    Science Advances   7 巻 ( 48 ) 頁: 1 - 22   2021年11月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Science Advances  

    Phytochromes constitute a widespread photoreceptor family that typically interconverts between two photostates called Pr (red light-absorbing) and Pfr (far-red light-absorbing). The lack of full-length structures solved at the (near-)atomic level in both pure Pr and Pfr states leaves gaps in the structural mechanisms involved in the signal transmission pathways during the photoconversion. Here, we present the crystallographic structures of three versions from the plant pathogen Xanthomonas campestris virulence regulator XccBphP bacteriophytochrome, including two full-length proteins, in the Pr and Pfr states. The structures show a reorganization of the interaction networks within and around the chromophore-binding pocket, an α-helix/β-sheet tongue transition, and specific domain reorientations, along with interchanging kinks and breaks at the helical spine as a result of the photoswitching, which subsequently affect the quaternary assembly. These structural findings, combined with multidisciplinary studies, allow us to describe the signaling mechanism of a full-length bacterial phytochrome at the atomic level.

    DOI: 10.1126/sciadv.abh1097

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  5. Pr-favoured variants of the bacteriophytochrome from the plant pathogen Xanthomonas campestris hint on light regulation of virulence-associated mechanisms 査読有り 国際誌

    Conforte V., Otero L.H., Toum L., Sirigu S., Antelo G.T., Rinaldi J., Foscaldi S., Klinke S., Chavas L.M.G., Vojnov A.A., Goldbaum F.A., Malamud F., Bonomi H.R.

    FEBS Journal   288 巻 ( 20 ) 頁: 5986 - 6002   2021年5月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:FEBS Journal  

    Red/far-red light-sensing bacteriophytochrome photoreceptor (BphP) pathways play key roles in bacterial physiology and ecology. These bilin-binding proteins photoswitch between two states, Pr (red absorbing) and Pfr (far-red absorbing). The isomerization of the chromophore and the downstream structural changes result in the light signal transduction. The agricultural pathogen Xanthomonas campestris pv. campestris (Xcc) code for a single bathy-like type BphP (XccBphP), previously shown to negatively regulate several light-mediated biological processes involved in virulence. Here, we generated three different full-length variants with single amino acid changes within its GAF domain that affect the XccBphP photocycle favouring its Pr state: L193Q, L193N and D199A. While D199A recombinant protein locks XccBphP in a Pr-like state, L193Q and L193N exhibit a significant enrichment of the Pr form in thermal equilibrium. The X-ray crystal structures of the three variants were solved, resembling the wild-type protein in the Pr state. Finally, we studied the effects of altering the XccBphP photocycle on the exopolysaccharide xanthan production and stomatal aperture assays as readouts of its bacterial signalling pathway. Null-mutant complementation assays show that the photoactive Pr-favoured XccBphP variants L193Q and L193N tend to negatively regulate xanthan production in vivo. In addition, our results indicate that strains expressing these variants also promote stomatal apertures in challenged plant epidermal peels, compared to wild-type Xcc. The findings presented in this work provide new evidence on the Pr state of XccBphP as a negative regulator of the virulence-associated mechanisms by light in Xcc.

    DOI: 10.1111/febs.15883

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    その他リンク: https://onlinelibrary.wiley.com/doi/full-xml/10.1111/febs.15883

  6. PROXIMA-1 beamline for macromolecular crystallography measurements at Synchrotron SOLEIL 査読有り 国際共著 国際誌

    Chavas L.M.G., Gourhant P., Guimaraes B.G., Isabet T., Legrand P., Lener R., Montaville P., Sirigu S., Thompson A.

    Journal of Synchrotron Radiation   28 巻 ( 3 ) 頁: 970 - 976   2021年5月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Journal of Synchrotron Radiation  

    The undulator beamline PROXIMA-1 at Synchrotron SOLEIL scheduled its first users in March 2008. The endstation is dedicated to biomolecular crystallography experiments, with a layout designed to favour anomalous data recording and studies of crystals with large cell dimensions. In 12 years, the beamline has accommodated 4267 shifts of 8 h and more than 6300 visitors. By the end of 2020, it saw 1039 identified published scientific papers referring to 1415 coordinates deposited in the Protein Data Bank. The current paper describes the PROXIMA-1 beamline, including the recent specific implementations developed for the sample environment. The setup installed in the experimental station contains numerous beam-shaping equipment, a chi-geometry three-axis goniometer, a single-photon-counting pixel-array X-ray detector, combined with a medium-throughput sample exchange robot. As part of a standard experimental scheme, PROXIMA-1 can also be accessed via 'mail-in' services or remotely.

    DOI: 10.1107/s1600577521002605

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  7. The microfluidic laboratory at Synchrotron SOLEIL. 国際誌

    Igor Chaussavoine, Anthony Beauvois, Tiphaine Mateo, Ramakrishna Vasireddi, Nadine Douri, Jordan Priam, Youssef Liatimi, Stéphane Lefrançois, Hervé Tabuteau, Mélanie Davranche, Delphine Vantelon, Thomas Bizien, Leonard M G Chavas, Benedikt Lassalle-Kaiser

    Journal of synchrotron radiation   27 巻 ( Pt 1 ) 頁: 230 - 237   2020年1月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    A microfluidic laboratory recently opened at Synchrotron SOLEIL, dedicated to in-house research and external users. Its purpose is to provide the equipment and expertise that allow the development of microfluidic systems adapted to the beamlines of SOLEIL as well as other light sources. Such systems can be used to continuously deliver a liquid sample under a photon beam, keep a solid sample in a liquid environment or provide a means to track a chemical reaction in a time-resolved manner. The laboratory provides all the amenities required for the design and preparation of soft-lithography microfluidic chips compatible with synchrotron-based experiments. Three examples of microfluidic systems that were used on SOLEIL beamlines are presented, which allow the use of X-ray techniques to study physical, chemical or biological phenomena.

    DOI: 10.1107/S1600577519015042

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  8. 欧州大型研究施設における統合生物学研究 招待有り 査読有り

      38 巻 ( 5 ) 頁: 858 - 862   2020年

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    担当区分:筆頭著者, 最終著者, 責任著者   記述言語:日本語   掲載種別:論文集(書籍)内論文  

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  9. Improvement of Production and Isolation of Human Neuraminidase-1 in Cellulo Crystals

    Kotaro Koiwai, Jun Tsukimoto, Tetsuya Higashi, Fumitaka Mafune, Ken Miyajima, Takanori Nakane, Naohiro Matsugaki, Ryuichi Kato, Serena Sirigu, Arjen Jakobi, Matthias Wilmanns, Michihiro Sugahara, Tomoyuki Tanaka, Kensuke Tono, Yasumasa Joti, Makina Yabashi, Osamu Nureki, Eiichi Mizohata, Toru Nakatsu, Eriko Nango, So Iwata, Leonard M. G. Chavas, Toshiya Senda, Kohji Itoh, Fumiaki Yumoto

    ACS APPLIED BIO MATERIALS   2 巻 ( 11 ) 頁: 4941 - 4952   2019年11月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:AMER CHEMICAL SOC  

    In cellulo crystallization is a developing technique to provide crystals for protein structure determination, particularly for proteins that are difficult to prepare by in vitro crystallization. This method has a key advantage: it requires neither a protein purification step nor a crystallization step. However, there is still no systematic strategy for improving the technique of in cellulo crystallization because the process occurs spontaneously. Here we report a protocol to produce and extract in cellulo crystals of human lysosomal neuraminidase-1 (NEU1) in human cultured cells. Overexpression of NEU1 protein by the retransfection of cells pretransfected with neu1-overexpressing plasmid improved the efficiency of NEU1 crystallization. Microscopic analysis revealed that NEU1 proteins were not crystallized in the lysosome but in the endoplasmic reticulum (ER). Screening of the buffer conditions used to extract crystals from cells further improved the crystal yield. The optimal pH was 7.0, which corresponds to the pH in the ER. Use of a high-yield flask with a large surface area also yielded more crystals. These optimizations enabled us to execute a serial femtosecond crystallography experiment with a sufficient number of crystals to generate a complete data set. Optimization of the in cellulo crystallization method was thus shown to be possible.

    DOI: 10.1021/acsabm.9b00686

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  10. Author Correction: Coherent diffractive imaging of microtubules using an X-ray laser. 国際誌

    Gisela Brändén, Greger Hammarin, Rajiv Harimoorthy, Alexander Johansson, David Arnlund, Erik Malmerberg, Anton Barty, Stefan Tångefjord, Peter Berntsen, Daniel P DePonte, Carolin Seuring, Thomas A White, Francesco Stellato, Richard Bean, Kenneth R Beyerlein, Leonard M G Chavas, Holger Fleckenstein, Cornelius Gati, Umesh Ghoshdastider, Lars Gumprecht, Dominik Oberthür, David Popp, Marvin Seibert, Thomas Tilp, Marc Messerschmidt, Garth J Williams, N Duane Loh, Henry N Chapman, Peter Zwart, Mengning Liang, Sébastien Boutet, Robert C Robinson, Richard Neutze

    Nature communications   10 巻 ( 1 ) 頁: 4101 - 4101   2019年9月

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    記述言語:英語   出版者・発行元:NATURE PUBLISHING GROUP  

    An amendment to this paper has been published and can be accessed via a link at the top of the paper.

    DOI: 10.1038/s41467-019-12151-3

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  11. Coherent diffractive imaging of microtubules using an X-ray laser. 国際誌

    Gisela Brändén, Greger Hammarin, Rajiv Harimoorthy, Alexander Johansson, David Arnlund, Erik Malmerberg, Anton Barty, Stefan Tångefjord, Peter Berntsen, Daniel P DePonte, Carolin Seuring, Thomas A White, Francesco Stellato, Richard Bean, Kenneth R Beyerlein, Leonard M G Chavas, Holger Fleckenstein, Cornelius Gati, Umesh Ghoshdastider, Lars Gumprecht, Dominik Oberthür, David Popp, Marvin Seibert, Thomas Tilp, Marc Messerschmidt, Garth J Williams, N Duane Loh, Henry N Chapman, Peter Zwart, Mengning Liang, Sébastien Boutet, Robert C Robinson, Richard Neutze

    Nature communications   10 巻 ( 1 ) 頁: 2589 - 2589   2019年6月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:NATURE PUBLISHING GROUP  

    X-ray free electron lasers (XFELs) create new possibilities for structural studies of biological objects that extend beyond what is possible with synchrotron radiation. Serial femtosecond crystallography has allowed high-resolution structures to be determined from micro-meter sized crystals, whereas single particle coherent X-ray imaging requires development to extend the resolution beyond a few tens of nanometers. Here we describe an intermediate approach: the XFEL imaging of biological assemblies with helical symmetry. We collected X-ray scattering images from samples of microtubules injected across an XFEL beam using a liquid microjet, sorted these images into class averages, merged these data into a diffraction pattern extending to 2 nm resolution, and reconstructed these data into a projection image of the microtubule. Details such as the 4 nm tubulin monomer became visible in this reconstruction. These results illustrate the potential of single-molecule X-ray imaging of biological assembles with helical symmetry at room temperature.

    DOI: 10.1038/s41467-019-10448-x

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  12. MXCuBE2: the dawn of MXCuBE Collaboration. 国際誌

    Marcus Oscarsson, Antonia Beteva, David Flot, Elspeth Gordon, Matias Guijarro, Gordon Leonard, Sean McSweeney, Stephanie Monaco, Christoph Mueller-Dieckmann, Max Nanao, Didier Nurizzo, Alexander N Popov, David von Stetten, Olof Svensson, Vicente Rey-Bakaikoa, Idrissou Chado, Leonard M G Chavas, Laurent Gadea, Patrick Gourhant, Tatiana Isabet, Pierre Legrand, Martin Savko, Serena Sirigu, William Shepard, Andrew Thompson, Uwe Mueller, Jie Nan, Mikel Eguiraun, Fredrick Bolmsten, Alberto Nardella, Antonio Milàn-Otero, Marjolein Thunnissen, Michael Hellmig, Alexandra Kastner, Lukas Schmuckermaier, Martin Gerlach, Christian Feiler, Manfred S Weiss, Matthew W Bowler, Alexandre Gobbo, Gergely Papp, Jeremy Sinoir, Andrew A McCarthy, Ivars Karpics, Marina Nikolova, Gleb Bourenkov, Thomas Schneider, Jordi Andreu, Guifré Cuní, Judith Juanhuix, Roeland Boer, Rasmus Fogh, Peter Keller, Claus Flensburg, Wlodek Paciorek, Clemens Vonrhein, Gerard Bricogne, Daniele de Sanctis

    Journal of synchrotron radiation   26 巻 ( Pt 2 ) 頁: 393 - 405   2019年3月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    MXCuBE2 is the second-generation evolution of the MXCuBE beamline control software, initially developed and used at ESRF - the European Synchrotron. MXCuBE2 extends, in an intuitive graphical user interface (GUI), the functionalities and data collection methods available to users while keeping all previously available features and allowing for the straightforward incorporation of ongoing and future developments. MXCuBE2 introduces an extended abstraction layer that allows easy interfacing of any kind of macromolecular crystallography (MX) hardware component, whether this is a diffractometer, sample changer, detector or optical element. MXCuBE2 also works in strong synergy with the ISPyB Laboratory Information Management System, accessing the list of samples available for a particular experimental session and associating, either from instructions contained in ISPyB or from user input via the MXCuBE2 GUI, different data collection types to them. The development of MXCuBE2 forms the core of a fruitful collaboration which brings together several European synchrotrons and a software development factory and, as such, defines a new paradigm for the development of beamline control platforms for the European MX user community.

    DOI: 10.1107/S1600577519001267

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  13. Diffracted X-ray Blinking Tracks Single Protein Motions. 国際誌

    Hiroshi Sekiguchi, Masahiro Kuramochi, Keigo Ikezaki, Yu Okamura, Kazuki Yoshimura, Ken Matsubara, Jae-Won Chang, Noboru Ohta, Tai Kubo, Kazuhiro Mio, Yoshio Suzuki, Leonard M G Chavas, Yuji C Sasaki

    Scientific reports   8 巻 ( 1 ) 頁: 17090 - 17090   2018年11月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:NATURE PUBLISHING GROUP  

    Single molecule dynamics studies have begun to use quantum probes. Single particle analysis using cryo-transmission electron microscopy has dramatically improved the resolution when studying protein structures and is shifting towards molecular motion observations. X-ray free-electron lasers are also being explored as routes for determining single molecule structures of biological entities. Here, we propose a new X-ray single molecule technology that allows observation of molecular internal motion over long time scales, ranging from milliseconds up to 103 seconds. Our method uses both low-dose monochromatic X-rays and nanocrystal labelling technology. During monochromatic X-ray diffraction experiments, the intensity of X-ray diffraction from moving single nanocrystals appears to blink because of Brownian motion in aqueous solutions. X-ray diffraction spots from moving nanocrystals were observed to cycle in and out of the Bragg condition. Consequently, the internal motions of a protein molecule labelled with nanocrystals could be extracted from the time trajectory using this diffracted X-ray blinking (DXB) approach. Finally, we succeeded in distinguishing the degree of fluctuation motions of an individual acetylcholine-binding protein (AChBP) interacting with acetylcholine (ACh) using a laboratory X-ray source.

    DOI: 10.1038/s41598-018-35468-3

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  14. The New Era of Microcrystallography

    Sanchari Banerjee, Pierre Montaville, Leonard M. G. Chavas, S. Ramaswamy

    JOURNAL OF THE INDIAN INSTITUTE OF SCIENCE   98 巻 ( 3 ) 頁: 273 - 281   2018年9月

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    記述言語:英語   出版者・発行元:SPRINGER  

    The function of a protein dictates its physical state in a cell. Evolution has imparted selection pressure on proteins to maximize their function and minimize cell death. Most of the proteins exist in their soluble form inside or outside the cells. However, a small fraction of proteins in the total protein pool crystallizes with functional consequence. These in vivo-grown protein crystals perform a diversity of functions, ranging from food storage to defense. Sometimes limited by the volume of the cells and the cellular concentration of proteins, these crystals are very small in size. Hence, it has been difficult to carry out conventional X-ray crystallography on these crystals. With the advent of microcrystallography, it is now possible to study the structures of these tiny crystals. In this review, some of the diverse examples of in vivo crystals and the new approaches towards microcrystallography are summarized.

    DOI: 10.1007/s41745-018-0086-0

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  15. Flow-aligned, single-shot fiber diffraction using a femtosecond X-ray free-electron laser. 国際誌

    David Popp, N Duane Loh, Habiba Zorgati, Umesh Ghoshdastider, Lu Ting Liow, Magdalena I Ivanova, Mårten Larsson, Daniel P DePonte, Richard Bean, Kenneth R Beyerlein, Cornelius Gati, Dominik Oberthuer, David Arnlund, Gisela Brändén, Peter Berntsen, Duilio Cascio, Leonard M G Chavas, Joe P J Chen, Ke Ding, Holger Fleckenstein, Lars Gumprecht, Rajiv Harimoorthy, Estelle Mossou, Michael R Sawaya, Aaron S Brewster, Johan Hattne, Nicholas K Sauter, Marvin Seibert, Carolin Seuring, Francesco Stellato, Thomas Tilp, David S Eisenberg, Marc Messerschmidt, Garth J Williams, Jason E Koglin, Lee Makowski, Rick P Millane, Trevor Forsyth, Sébastien Boutet, Thomas A White, Anton Barty, Henry Chapman, Swaine L Chen, Mengning Liang, Richard Neutze, Robert C Robinson

    Cytoskeleton (Hoboken, N.J.)   74 巻 ( 12 ) 頁: 472 - 481   2017年12月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:WILEY  

    A major goal for X-ray free-electron laser (XFEL) based science is to elucidate structures of biological molecules without the need for crystals. Filament systems may provide some of the first single macromolecular structures elucidated by XFEL radiation, since they contain one-dimensional translational symmetry and thereby occupy the diffraction intensity region between the extremes of crystals and single molecules. Here, we demonstrate flow alignment of as few as 100 filaments (Escherichia coli pili, F-actin, and amyloid fibrils), which when intersected by femtosecond X-ray pulses result in diffraction patterns similar to those obtained from classical fiber diffraction studies. We also determine that F-actin can be flow-aligned to a disorientation of approximately 5 degrees. Using this XFEL-based technique, we determine that gelsolin amyloids are comprised of stacked β-strands running perpendicular to the filament axis, and that a range of order from fibrillar to crystalline is discernable for individual α-synuclein amyloids.

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  16. Post-sample aperture for low background diffraction experiments at X-ray free-electron lasers. 国際誌

    Max O Wiedorn, Salah Awel, Andrew J Morgan, Miriam Barthelmess, Richard Bean, Kenneth R Beyerlein, Leonard M G Chavas, Niko Eckerskorn, Holger Fleckenstein, Michael Heymann, Daniel A Horke, Juraj Knoška, Valerio Mariani, Dominik Oberthür, Nils Roth, Oleksandr Yefanov, Anton Barty, Saša Bajt, Jochen Küpper, Andrei V Rode, Richard A Kirian, Henry N Chapman

    Journal of synchrotron radiation   24 巻 ( Pt 6 ) 頁: 1296 - 1298   2017年11月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    The success of diffraction experiments from weakly scattering samples strongly depends on achieving an optimal signal-to-noise ratio. This is particularly important in single-particle imaging experiments where diffraction signals are typically very weak and the experiments are often accompanied by significant background scattering. A simple way to tremendously reduce background scattering by placing an aperture downstream of the sample has been developed and its application in a single-particle X-ray imaging experiment at FLASH is demonstrated. Using the concept of a post-sample aperture it was possible to reduce the background scattering levels by two orders of magnitude.

    DOI: 10.1107/S1600577517011961

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  17. Crystallization via tubing microfluidics permits both in situ and ex situ X-ray diffraction 国際誌

    Charline J. J. Gerard, Gilles Ferry, Laurent M. Vuillard, Jean A. Boutin, Leonard M. G. Chavas, Tiphaine Huet, Nathalie Ferte, Romain Grossier, Nadine Candoni, Stéphane Veesler

    Acta Crystallographica Section F Structural Biology Communications   73 巻 ( 10 ) 頁: 574 - 578   2017年10月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:International Union of Crystallography ({IUCr})  

    A microfluidic platform was used to address the problems of obtaining diffraction-quality crystals and crystal handling during transfer to the X-ray diffractometer. Crystallization conditions of a protein of pharmaceutical interest were optimized and X-ray data were collected both in situ and ex situ.

    DOI: 10.1107/S2053230X17013826

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  18. The impact of the butterfly effect on human parainfluenza virus haemagglutinin-neuraminidase inhibitor design. 国際誌

    Larissa Dirr, Ibrahim M El-Deeb, Leonard M G Chavas, Patrice Guillon, Mark von Itzstein

    Scientific reports   7 巻 ( 1 ) 頁: 4507 - 4507   2017年7月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:NATURE PUBLISHING GROUP  

    Human parainfluenza viruses represent a leading cause of lower respiratory tract disease in children, with currently no available approved drug or vaccine. The viral surface glycoprotein haemagglutinin-neuraminidase (HN) represents an ideal antiviral target. Herein, we describe the first structure-based study on the rearrangement of key active site amino acid residues by an induced opening of the 216-loop, through the accommodation of appropriately functionalised neuraminic acid-based inhibitors. We discovered that the rearrangement is influenced by the degree of loop opening and is controlled by the neuraminic acid's C-4 substituent's size (large or small). In this study, we found that these rearrangements induce a butterfly effect of paramount importance in HN inhibitor design and define criteria for the ideal substituent size in two different categories of HN inhibitors and provide novel structural insight into the druggable viral HN protein.

    DOI: 10.1038/s41598-017-04656-y

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  19. Status of the crystallography beamlines at synchrotron SOLEIL⋆

    A. Coati, L. M. G. Chavas, P. Fontaine, N. Foos, B. Guimaraes, P. Gourhant, P. Legrand, J. -P. Itie, P. Fertey, W. Shepard, T. Isabet, S. Sirigu, P. -L. Solari, D. Thiaudiere, A. Thompson

    The European Physical Journal Plus   132 巻 ( 4 )   2017年4月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Springer Science and Business Media LLC  

    DOI: 10.1140/epjp/i2017-11403-3

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  20. Role of Quinone Reductase 2 in the Antimalarial Properties of Indolone-Type Derivatives. 国際誌

    Laure-Estelle Cassagnes, Nambinina Rakotoarivelo, Serena Sirigu, Pierre Pério, Ennaji Najahi, Léonard M G Chavas, Andrew Thompson, Régis Gayon, Gilles Ferry, Jean A Boutin, Alexis Valentin, Karine Reybier, Françoise Nepveu

    Molecules (Basel, Switzerland)   22 巻 ( 2 )   2017年1月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:MDPI AG  

    Indolone-N-oxides have antiplasmodial properties against Plasmodium falciparum at the erythrocytic stage, with IC50 values in the nanomolar range. The mechanism of action of indolone derivatives involves the production of free radicals, which follows their bioreduction by an unknown mechanism. In this study, we hypothesized that human quinone reductase 2 (hQR2), known to act as a flavin redox switch upon binding to the broadly used antimalarial chloroquine, could be involved in the activity of the redox-active indolone derivatives. Therefore, we investigated the role of hQR2 in the reduction of indolone derivatives. We analyzed the interaction between hQR2 and several indolone-type derivatives by examining enzymatic kinetics, the substrate/protein complex structure with X-ray diffraction analysis, and the production of free radicals with electron paramagnetic resonance. The reduction of each compound in cells overexpressing hQR2 was compared to its reduction in naïve cells. This process could be inhibited by the specific hQR2 inhibitor, S29434. These results confirmed that the anti-malarial activity of indolone-type derivatives was linked to their ability to serve as hQR2 substrates and not as hQR2 inhibitors as reported for chloroquine, leading to the possibility that substrate of hQR2 could be considered as a new avenue for the design of new antimalarial compounds.

    DOI: 10.3390/molecules22020210

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  21. De novo in-vivo protein crystal structure: is experimental phasing required?

    Pierre Montaville, Leonard Chavas

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   73 巻   頁: C878 - C878   2017年

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    記述言語:英語   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    DOI: 10.1107/S205327331708696X

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  22. Structure of in vivo protein crystals from viviparous Diploptera punctata

    Sanchari Banerjee, Nathan P. Coussens, Francois-Xavier Gallat, Nitish Sathyanarayanan, Koichiro J. Yagi, James S. S. Gray, Stephen S. Tobe, Barbara Stay, Leonard M. G. Chavas, S. Ramaswamy

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   73 巻   頁: C177 - C177   2017年

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    記述言語:英語   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    DOI: 10.1107/S2053273317093962

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  23. Total chemical synthesis, refolding, and crystallographic structure of fully active immunophilin calstabin 2 (FKBP12.6). 国際誌

    Marine Bacchi, Magali Jullian, Serena Sirigu, Benjamin Fould, Tiphaine Huet, Lisa Bruyand, Mathias Antoine, Laurent Vuillard, Luisa Ronga, Leonard M G Chavas, Olivier Nosjean, Gilles Ferry, Karine Puget, Jean A Boutin

    Protein science : a publication of the Protein Society   25 巻 ( 12 ) 頁: 2225 - 2242   2016年12月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:WILEY-BLACKWELL  

    Synthetic biology (or chemical biology) is a growing field to which the chemical synthesis of proteins, particularly enzymes, makes a fundamental contribution. However, the chemical synthesis of catalytically active proteins (enzymes) remains poorly documented because it is difficult to obtain enough material for biochemical experiments. We chose calstabin, a 107-amino-acid proline isomerase, as a model. We synthesized the enzyme using the native chemical ligation approach and obtained several tens of milligrams. The polypeptide was refolded properly, and we characterized its biophysical properties, measured its catalytic activity, and then crystallized it in order to obtain its tridimensional structure after X-ray diffraction. The refolded enzyme was compared to the recombinant, wild-type enzyme. In addition, as a first step of validating the whole process, we incorporated exotic amino acids into the N-terminus. Surprisingly, none of the changes altered the catalytic activities of the corresponding mutants. Using this body of techniques, avenues are now open to further obtain enzymes modified with exotic amino acids in a way that is only barely accessible by molecular biology, obtaining detailed information on the structure-function relationship of enzymes reachable by complete chemical synthesis.

    DOI: 10.1002/pro.3051

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  24. Structure of a heterogeneous, glycosylated, lipid-bound, in vivo-grown protein crystal at atomic resolution from the viviparous cockroach Diploptera punctata. 国際誌

    Sanchari Banerjee, Nathan P Coussens, François-Xavier Gallat, Nitish Sathyanarayanan, Jandhyam Srikanth, Koichiro J Yagi, James S S Gray, Stephen S Tobe, Barbara Stay, Leonard M G Chavas, Subramanian Ramaswamy

    IUCrJ   3 巻 ( Pt 4 ) 頁: 282 - 93   2016年7月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Macromolecular crystals for X-ray diffraction studies are typically grown in vitro from pure and homogeneous samples; however, there are examples of protein crystals that have been identified in vivo. Recent developments in micro-crystallography techniques and the advent of X-ray free-electron lasers have allowed the determination of several protein structures from crystals grown in cellulo. Here, an atomic resolution (1.2 Å) crystal structure is reported of heterogeneous milk proteins grown inside a living organism in their functional niche. These in vivo-grown crystals were isolated from the midgut of an embryo within the only known viviparous cockroach, Diploptera punctata. The milk proteins crystallized in space group P1, and a structure was determined by anomalous dispersion from the native S atoms. The data revealed glycosylated proteins that adopt a lipocalin fold, bind lipids and organize to form a tightly packed crystalline lattice. A single crystal is estimated to contain more than three times the energy of an equivalent mass of dairy milk. This unique storage form of nourishment for developing embryos allows access to a constant supply of complete nutrients. Notably, the crystalline cockroach-milk proteins are highly heterogeneous with respect to amino-acid sequence, glycosylation and bound fatty-acid composition. These data present a unique example of protein heterogeneity within a single in vivo-grown crystal of a natural protein in its native environment at atomic resolution.

    DOI: 10.1107/S2052252516008903

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  25. Industrial integration at the French national synchrotron facility SOLEIL

    Tiphaine Huet, Gilbert Bey, Laurent M. Vuillard, Gilles Ferry, Leonard M. G. Chavas, Andrew W. Thompson

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   72 巻   頁: S206 - S206   2016年

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    記述言語:英語   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    DOI: 10.1107/S205327331609690X

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  26. Possibilities for serial femtosecond crystallography sample delivery at future light sourcesa)

    L. M. G. Chavas, L. Gumprecht, H. N. Chapman

    Structural Dynamics   2 巻 ( 4 ) 頁: 041709 - 041709   2015年7月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:AIP Publishing  

    DOI: 10.1063/1.4921220

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  27. Simple convergent-nozzle aerosol injector for single-particle diffractive imaging with X-ray free-electron lasers

    R. A. Kirian, S. Awel, N. Eckerskorn, H. Fleckenstein, M. Wiedorn, L. Adriano, S. Bajt, M. Barthelmess, R. Bean, K. R. Beyerlein, L. M. G. Chavas, M. Domaracky, M. Heymann, D. A. Horke, J. Knoska, M. Metz, A. Morgan, D. Oberthuer, N. Roth, T. Sato, P. L. Xavier, O. Yefanov, A. V. Rode, J. Küpper, H. N. Chapman

    Structural Dynamics   2 巻 ( 4 ) 頁: 041717 - 041717   2015年7月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:AIP Publishing  

    DOI: 10.1063/1.4922648

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  28. The catalytic mechanism of human parainfluenza virus type 3 haemagglutinin-neuraminidase revealed. 国際誌

    Larissa Dirr, Ibrahim M El-Deeb, Patrice Guillon, Cindy J Carroux, Leonard M G Chavas, Mark von Itzstein

    Angewandte Chemie (International ed. in English)   54 巻 ( 10 ) 頁: 2936 - 40   2015年3月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:WILEY-V C H VERLAG GMBH  

    Human parainfluenza virus type 3 (hPIV-3) is one of the leading causes for lower respiratory tract disease in children, with neither an approved antiviral drug nor vaccine available to date. Understanding the catalytic mechanism of human parainfluenza virus haemagglutinin-neuraminidase (HN) protein is key to the design of specific inhibitors against this virus. Herein, we used (1) H NMR spectroscopy, X-ray crystallography, and virological assays to study the catalytic mechanism of the HN enzyme activity and have identified the conserved Tyr530 as a key amino acid involved in catalysis. A novel 2,3-difluorosialic acid derivative showed prolonged enzyme inhibition and was found to react and form a covalent bond with Tyr530. Furthermore, the novel derivative exhibited enhanced potency in virus blockade assays relative to its Neu2en analogue. These outcomes open the door for a new generation of potent inhibitors against hPIV-3 HN.

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  29. Serial femtosecond crystallography on in vivo grown crystals at SACLA - developments and results 招待有り 査読有り 国際共著 国際誌

    Leonard M. G. Chavas, Sasa Bajt, Lars Gumprecht, Henry N. Chapman

    Acta Crystallographica Section A Foundations and Advances   71 巻   頁: S148 - S148   2015年

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    担当区分:筆頭著者, 責任著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Serial femtosecond crystallography on in vivo grown crystals at SACLA - developments and results

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  30. AGIPD detector for Serial Femtosecond Crystallography Apparatus at European XFEL 招待有り 査読有り 国際共著 国際誌

    Stephan Stern, Leonard Chavas, Henry Chapman, Adrian Mancuso, Andrew Aquila, Klaus Giewekemeyer, Julian Becker, Heinz Graafsma, Bernd Schmitt

    Acta Crystallographica Section A Foundations and Advances   70 巻 ( a1 ) 頁: C694 - C694   2014年8月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    The European X-ray Free-Electron Laser (XFEL.EU) [1] will provide ultra-short, highly-intense, coherent x-ray pulses at an unprecedented repetition rate, transforming experiments in many scientific areas, including serial femtosecond crystallography (SFX). For the purpose of SFX experiments at the XFEL.EU, a dedicated endstation is being developed to be installed within the Single Particles, Clusters and Biomolecules (SPB) instrument [2]. The setup will refocus the beam spent by SPB into a second interaction region, thereby enabling two parallel experiments. In order to overcome various challenges in XFEL crystallography, and to optimize the output for SFX experiments at XFEL.EU, the Adaptive Gain Integrating Pixel Detector (AGIPD) [3] is currently under development and is to be implemented in the SPB instrument, including a 4 Megapixel version for the SFX apparatus. The AGIPD is a hybrid-pixel detector with pixels of 200 x 200 micron^2 each. The gain of each single pixel dynamically and independently adapts to the incoming signal. Thus, diffraction patterns of high dynamic range can be recorded, with the measured signal within a single data frame ranging from single photons and up to 1e+4 photons at 12 keV. Moreover, the AGIPD is designed to store over 350 data frames from successive pulses prior to digitization and read-out, thereby enabling operation at the European XFEL with its challenging repetition rate with 10 Hz pulse trains and a 4.5 MHz intra-train repetition rate. Furthermore, the incorporation of a veto system in AGIPD will allow one to potentially store only the frames that contain diffraction data from actual crystal hits, which ultimately increases the efficiency of the detector and DAQ systems dramatically. In the present work, we will review the design of the 4Mpix AGIPD for the SFX apparatus and discuss simulations and tests of its expected performance under the conditions foreseen for SFX experiments at the XFEL.EU.

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  31. Serial Femtosecond Crystallography user's consortium apparatus at European XFEL 招待有り 査読有り 国際共著 国際誌

    Marc Messerschmidt, Leonard Chavas, Sunil Ananthaneni, Hamidreza Dadgostar, Heinz Graafsma, Mengning Liang, Adrian Mancuso, Steffen Raabe, Stephan Stern, Patrik Vagovic, Henry Chapman

    Acta Crystallographica Section A Foundations and Advances   70 巻 ( a1 ) 頁: C1748 - C1748   2014年8月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    The Serial Femtosecond Crystallography (SFX) user's consortium apparatus is to be installed within the Single Particles, Clusters and Biomolecules (SPB) instrument of the European X-ray Free-Electron Laser facility (XFEL.EU) [1, 2]. The XFEL.EU will provide ultra-short, highly intense, coherent X-ray pulses at an unprecedented repetition rate. The experimental setup and methodological approaches of many scientific areas will be transformed, including structural biology that could potentially overcome common problems and bottlenecks encountered in crystallography, such as creating large crystals, dealing with radiation damage, or understanding sub-picosecond time-resolved phenomena. The key concept of the SFX method is based on the kinetic insertion of protein crystal samples in solution via a gas dynamic virtual nozzle jet and recording diffraction signals of individual, randomly oriented crystals passing through the XFEL beam, as first demonstrated by Chapman et al. [3]. The SFX-apparatus will refocus the beam spent by the SPB instrument into a second interaction region, in some cases enabling two parallel experiments. The planned photon energy range at the SPB instrument is from 3 to 16 keV. The Adaptive Gain Integrating Pixel Detector (AGIPD) is to be implemented in the SPB instrument, including a 4 Megapixel version for the SFX-apparatus. The AGIPD is designed to store over 350 data frames from successive pulses, and aims to collect more than 3,000 images per second. Together with the implementation of automated procedures for sample exchange and injection, high-throughput nanocrystallography experiments can be integrated at the SFX-apparatus. In this work, we review the overall design of the SFX-apparatus and discuss the main parameters and challenges

    DOI: 10.1107/s2053273314082515

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  32. In vivo crystallography at X-ray free-electron lasers: the next generation of structural biology? 査読有り 国際共著 国際誌

    François-Xavier Gallat, Naohiro Matsugaki, Nathan P Coussens, Koichiro J Yagi, Marion Boudes, Tetsuya Higashi, Daisuke Tsuji, Yutaka Tatano, Mamoru Suzuki, Eiichi Mizohata, Kensuke Tono, Yasumasa Joti, Takashi Kameshima, Jaehyun Park, Changyong Song, Takaki Hatsui, Makina Yabashi, Eriko Nango, Kohji Itoh, Fasséli Coulibaly, Stephen Tobe, S Ramaswamy, Barbara Stay, So Iwata, Leonard M G Chavas

    Philosophical transactions of the Royal Society of London. Series B, Biological sciences   369 巻 ( 1647 ) 頁: 20130497 - 20130497   2014年7月

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    担当区分:最終著者, 責任著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:ROYAL SOC  

    The serendipitous discovery of the spontaneous growth of protein crystals inside cells has opened the field of crystallography to chemically unmodified samples directly available from their natural environment. On the one hand, through in vivo crystallography, protocols for protein crystal preparation can be highly simplified, although the technique suffers from difficulties in sampling, particularly in the extraction of the crystals from the cells partly due to their small sizes. On the other hand, the extremely intense X-ray pulses emerging from X-ray free-electron laser (XFEL) sources, along with the appearance of serial femtosecond crystallography (SFX) is a milestone for radiation damage-free protein structural studies but requires micrometre-size crystals. The combination of SFX with in vivo crystallography has the potential to boost the applicability of these techniques, eventually bringing the field to the point where in vitro sample manipulations will no longer be required, and direct imaging of the crystals from within the cells will be achievable. To fully appreciate the diverse aspects of sample characterization, handling and analysis, SFX experiments at the Japanese SPring-8 angstrom compact free-electron laser were scheduled on various types of in vivo grown crystals. The first experiments have demonstrated the feasibility of the approach and suggest that future in vivo crystallography applications at XFELs will be another alternative to nano-crystallography.

    DOI: 10.1098/rstb.2013.0497

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  33. Small Angle X-Ray and Neutron Scattering from Solutions of Biological Macromolecules. By Dmitri I. Svergun, Michel H. J. Koch, Peter A. Timmins and Roland P. May. IUCr Texts on Crystallography, No. 19. Oxford University Press, 2013. Pp. 358. Price (hardback) £49.99. ISBN: 978-0-19-963953-3. 招待有り 査読有り 国際誌

    Leonard Michel Gabriel Chavas

    Acta Crystallographica Section D Biological Crystallography   70 巻 ( 4 ) 頁: 1175 - 1176   2014年4月

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    担当区分:筆頭著者, 最終著者, 責任著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Small Angle X-ray and Neutron Scattering from Solutions of Biological Macromolecules is a superb book that efficiently summarises both SAXS (small-angle X-ray scattering) and SANS (small-angle neutron scattering) techniques in a flow driven by the ambition to bring readers from an inexperienced background to a good practical knowledge and understanding of these scattering methods.

    DOI: 10.1107/s1399004714005719

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  34. Tuning mechanism-based inactivators of neuraminidases: mechanistic and structural insights. 査読有り 国際共著 国際誌

    Sabrina Buchini, François-Xavier Gallat, Ian R Greig, Jin-Hyo Kim, Soichi Wakatsuki, Leonard M G Chavas, Stephen G Withers

    Angewandte Chemie (International ed. in English)   53 巻 ( 13 ) 頁: 3382 - 6   2014年3月

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    担当区分:責任著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Wiley-VCH (Germany)  

    3-Fluorosialosyl fluorides are inhibitors of sialidases that function by the formation of a long-lived covalent active-site adduct and have potential as therapeutics if made specific for the pathogen sialidase. Surprisingly, human Neu2 and the Trypanosoma cruzi trans-sialidase are inactivated more rapidly by the reagent with an equatorial fluorine at C3 than by its axial epimer, with reactivation following the same pattern. To explore a possible stereoelectronic basis for this, rate constants for spontaneous hydrolysis of the full series of four 3-fluorosialosyl fluorides were measured, and ground-state energies for each computed. The alpha (equatorial) anomeric fluorides hydrolyze more rapidly than their beta anomers, consistent with their higher ground-state energies. However ground-state energies do not explain the relative spontaneous reactivities of the 3-fluoro-epimers. The three-dimensional structures of the two 3-fluoro-sialosyl enzyme intermediates of human Neu2 were solved, revealing key stabilizing interactions between Arg21 and the equatorial, but not the axial, fluorine. Because of changes in geometry these interactions will increase at the transition state, likely explaining the difference in reaction rates.

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  35. Improvement of an automated protein crystal exchange system PAM for high-throughput data collection. 査読有り 国際誌

    Masahiko Hiraki, Yusuke Yamada, Leonard M G Chavas, Soichi Wakatsuki, Naohiro Matsugaki

    Journal of synchrotron radiation   20 巻 ( Pt 6 ) 頁: 890 - 3   2013年11月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Photon Factory Automated Mounting system (PAM) protein crystal exchange systems are available at the following Photon Factory macromolecular beamlines: BL-1A, BL-5A, BL-17A, AR-NW12A and AR-NE3A. The beamline AR-NE3A has been constructed for high-throughput macromolecular crystallography and is dedicated to structure-based drug design. The PAM liquid-nitrogen Dewar can store a maximum of three SSRL cassettes. Therefore, users have to interrupt their experiments and replace the cassettes when using four or more of them during their beam time. As a result of investigation, four or more cassettes were used in AR-NE3A alone. For continuous automated data collection, the size of the liquid-nitrogen Dewar for the AR-NE3A PAM was increased, doubling the capacity. In order to check the calibration with the new Dewar and the cassette stand, calibration experiments were repeatedly performed. Compared with the current system, the parameters of the novel system are shown to be stable.

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  36. New methodologies at PF AR-NW12A: The implementation of high-pressure macromolecular crystallography 査読有り 国際誌

    Leonard Michel Gabriel Chavas, Tadayuki Nagae, Hiroyuki Yamada, Nobuhisa Watanabe, Yusuke Yamada, Masahiko Hiraki, Naohiro Matsugaki

    Journal of Synchrotron Radiation   20 巻 ( Pt 6 ) 頁: 838 - 42   2013年11月

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    担当区分:筆頭著者, 責任著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    The macromolecular crystallography (MX) beamline AR-NW12A is evolving from its original design of high-throughput crystallography to a multi-purpose end-station. Among the various options to be implemented, great efforts were made in making available high-pressure MX (HPMX) at the beamline. High-pressure molecular biophysics is a developing field that attracts the interest of a constantly growing scientific community. A plethora of activities can benefit from high pressure, and investigations have been performed on its applicability to study multimeric complex assemblies, compressibility of proteins and their crystals, macromolecules originating from extremophiles, or even the trapping of higher-energy conformers for molecules of biological interest. Recent studies using HPMX showed structural hydrostatic-pressure-induced changes in proteins. The conformational modifications could explain the enzymatic mechanism differences between proteins of the same family, living at different environmental pressures, as well as the initial steps in the pressure-denaturation process that have been attributed to water penetration into the protein interior. To facilitate further HPMX, while allowing access to various individualized set-ups and experiments, the AR-NW12A sample environment has been revisited. Altogether, the newly added implementations will bring a fresh breath of life to AR-NW12A and allow the MX community to experiment in a larger set of fields related to structural biology.

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  37. Improvements toward highly accurate diffraction experiments at the macromolecular micro-crystallography beamline BL-17A. 査読有り 国際誌

    Yusuke Yamada, Leonard M G Chavas, Noriyuki Igarashi, Masahiko Hiraki, Soichi Wakatsuki, Naohiro Matsugaki

    Journal of synchrotron radiation   20 巻 ( Pt 6 ) 頁: 938 - 42   2013年11月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    BL-17A is a macromolecular crystallography beamline dedicated to diffraction experiments conducted using micro-crystals and structure determination studies using a lower energy X-ray beam. In these experiments, highly accurate diffraction intensity measurements are definitively important. Since this beamline was constructed, the beamline apparatus has been improved in several ways to enable the collection of accurate diffraction data. The stability of the beam intensities at the sample position was recently improved by modifying the monochromator. The diffractometer has also been improved. A new detector table was installed to prevent distortions in the diffractometer's base during the repositioning of the diffractometer detector. A new pinhole system and an on-axis viewing system were installed to improve the X-ray beam profile at the sample position and the centering of tiny crystal samples.

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  38. 10 years of protein crystallography at AR-NW12A beamline 招待有り 査読有り

    L M G Chavas, Y Yamada, M Hiraki, N Igarashi, N Matsugaki, S Wakatsuki

    Journal of Physics: Conference Series   425 巻 ( 1 ) 頁: 012008 - 012008   2013年3月

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    担当区分:筆頭著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:IOP Publishing  

    10 years of protein crystallography at AR-NW12A beamline

    DOI: 10.1088/1742-6596/425/1/012008

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  39. Data Management System at the Photon Factory Macromolecular Crystallography Beamline 招待有り 査読有り 国際誌

    Y Yamada, N Matsugaki, L M G Chavas, M Hiraki, N Igarashi, S Wakatsuki

    Journal of Physics: Conference Series   425 巻 ( 1 ) 頁: 012017 - 012017   2013年3月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:IOP Publishing  

    Data Management System at the Photon Factory Macromolecular Crystallography Beamline

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  40. Current status and future prospects of an automated sample exchange system PAM for protein crystallography 招待有り 査読有り 国際誌

    M Hiraki, Y Yamada, L M G Chavas, N Matsugaki, N Igarashi, S Wakatsuki

    Journal of Physics: Conference Series   425 巻 ( 1 ) 頁: 012014 - 012014   2013年3月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:IOP Publishing  

    Current status and future prospects of an automated sample exchange system PAM for protein crystallography

    DOI: 10.1088/1742-6596/425/1/012014

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  41. 1P001 高エネ機構フォトンファクトリーにおける創薬等支援基盤プラットフォーム事業による構造生物学研究の支援と高度化(01A. 蛋白質:構造,ポスター,日本生物物理学会年会第51回(2013年度)) 査読有り

    Kato Ryuichi, Matsugaki Naohiro, Yamada Yusuke, Chavas Leonard, Yumoto Fumiaki, Kawasaki Masato, Hiraki Masahiko, Senda Toshiya

    生物物理   53 巻 ( 1 ) 頁: S106   2013年

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:一般社団法人 日本生物物理学会  

    高エネ機構フォトンファクトリーにおける創薬等支援基盤プラットフォーム事業による構造生物学研究の支援と高度化

    DOI: 10.2142/biophys.53.S106_1

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  42. Beamline AR-NW12A: high-throughput beamline for macromolecular crystallography at the Photon Factory 査読有り

    L. M. G. Chavas, N. Matsugaki, Y. Yamada, M. Hiraki, N. Igarashi, M. Suzuki, S. Wakatsuki

    Journal of Synchrotron Radiation   19 巻 ( 3 ) 頁: 450 - 454   2012年5月

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    担当区分:筆頭著者, 責任著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    AR-NW12A is an in-vacuum undulator beamline optimized for high-throughput macromolecular crystallography experiments as one of the five macromolecular crystallography (MX) beamlines at the Photon Factory. This report provides details of the beamline design, covering its optical specifications, hardware set-up, control software, and the latest developments for MX experiments. The experimental environment presents state-of-the-art instrumentation for high-throughput projects with a high-precision goniometer with an adaptable goniometer head, and a UV-light sample visualization system. Combined with an efficient automounting robot modified from the SSRL SAM system, a remote control system enables fully automated and remote-access X-ray diffraction experiments.

    DOI: 10.1107/s0909049512009727

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  43. High-pressure-induced water penetration into 3-isopropylmalate dehydrogenase 査読有り 国際誌

    Takayuki Nagae, Takashi Kawamura, Leonard M G Chavas, Ken Niwa, Masashi Hasegawa, Chiaki Kato, Nobuhisa Watanabe

    Acta Crystallographica Section D: Biological Crystallography   68 巻 ( Pt 3 ) 頁: 300 - 9   2012年3月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Hydrostatic pressure induces structural changes in proteins, including denaturation, the mechanism of which has been attributed to water penetration into the protein interior. In this study, structures of 3-isopropylmalate dehydrogenase (IPMDH) from Shewanella oneidensis MR-1 were determined at about 2 Å resolution under pressures ranging from 0.1 to 650 MPa using a diamond anvil cell (DAC). Although most of the protein cavities are monotonically compressed as the pressure increases, the volume of one particular cavity at the dimer interface increases at pressures over 340 MPa. In parallel with this volume increase, water penetration into the cavity could be observed at pressures over 410 MPa. In addition, the generation of a new cleft on the molecular surface accompanied by water penetration could also be observed at pressures over 580 MPa. These water-penetration phenomena are considered to be initial steps in the pressure-denaturation process of IPMDH. © 2012 International Union of Crystallography Printed in Singapore - all rights reserved.

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  44. Structural biology beamlines at the Photon Factory 招待有り 査読有り 国際誌

    Yusuke Yamada, Naohiro Matsugaki, Leonard M. G. Chavas, Masahiko Hiraki, Nobutaka Shimizu, Noriyuki Igarashi, Soichi Wakatsuki

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   68 巻   頁: S148 - S148   2012年

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    記述言語:英語   掲載種別:研究論文(国際会議プロシーディングス)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Structural biology beamlines at the Photon Factory

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  45. UV LED lighting for automated crystal centring. 査読有り 国際誌

    Leonard M G Chavas, Yusuke Yamada, Masahiko Hiraki, Noriyuki Igarashi, Naohiro Matsugaki, Soichi Wakatsuki

    Journal of synchrotron radiation   18 巻 ( 1 ) 頁: 11 - 5   2011年1月

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    担当区分:筆頭著者, 責任著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    A direct outcome of the exponential growth of macromolecular crystallography is the continuously increasing demand for synchrotron beam time, both from academic and industrial users. As more and more projects entail screening a profusion of sample crystals, fully automated procedures at every level of the experiments are being implemented at all synchrotron facilities. One of the major obstacles to achieving such automation lies in the sample recognition and centring in the X-ray beam. The capacity of UV light to specifically react with aromatic residues present in proteins or with DNA base pairs is at the basis of UV-assisted crystal centring. Although very efficient, a well known side effect of illuminating biological samples with strong UV sources is the damage induced on the irradiated samples. In the present study the effectiveness of a softer UV light for crystal centring by taking advantage of low-power light-emitting diode (LED) sources has been investigated. The use of UV LEDs represents a low-cost solution for crystal centring with high specificity.

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  46. Low energy SAD experiments performed at the photon factory BL-1A 招待有り 査読有り 国際誌

    Naohiro Matsugaki, Yusuke Yamada, Leonard M. G. Chavas, Masahiko Hiraki, Masato Kawasaki, Ryuichi Kato, Noriyuki Igarashi, Soichi Wakatsuki

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   67 巻   頁: C355 - C355   2011年

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    記述言語:英語   掲載種別:研究論文(国際会議プロシーディングス)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

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  47. Structure study of IPMDH from piezosensitive and piezophilic Shewanella species 招待有り 査読有り 国際誌

    Takayuki Nagae, Takashi Kawamura, Leonard Chavas, Ken Niwa, Masashi Hasegawa, Chiaki Kato, Nobuhisa Watanabe

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   67 巻   頁: C275 - C276   2011年

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    記述言語:英語   掲載種別:研究論文(国際会議プロシーディングス)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    DOI: 10.1107/S0108767311093111

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  48. Structural biology and SAXS beamlines at the photon factory 招待有り 査読有り 国際誌

    Noriyuki Igarashi, Naohiro Matsugaki, Yusuke Yamada, Leonard G. M. Chavas, Masahiko Hiraki, Nobutaka Shimizu, Takeharu Mori, Soichi Wakatsuki

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   67 巻   頁: C803 - C803   2011年

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    記述言語:英語   掲載種別:研究論文(国際会議プロシーディングス)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Structural biology and SAXS beamlines at the photon factory

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  49. Potential of UV in phasing and its implementation for crystal centering at PF 招待有り 査読有り 国際誌

    Leonard M. G. Chavas, Yusuke Yamada, Masahiro Hiraki, Seiji Okazaki, Noriyuki Igarashi, Naohiro Matsugaki, Soichi Wakatsuki

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   67 巻   頁: C656 - C656   2011年

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    記述言語:英語   掲載種別:研究論文(国際会議プロシーディングス)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Potential of UV in phasing and its implementation for crystal centering at PF

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  50. ターゲットタンパク研究プログラムで目指すX線構造解析の高度化:フォトンファクトリーにおける技術開発 招待有り 査読有り

    若槻 壮市, 山田 悠介, Leonard M. G. CHAVAS, 五十嵐 教之, 川崎 政人, 加藤 龍一, 平木 雅彦, 松垣 直宏

    Yakugaku zasshi   130 巻 ( 5 ) 頁: 631 - 40   2010年5月

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    記述言語:日本語   掲載種別:研究論文(学術雑誌)   出版者・発行元:PHARMACEUTICAL SOC JAPAN  

    The Targeted Protein Research Program (TPRP) started in 2007 as a sequel of the Protein 3000 Project which lasted from 2002 to 2007. In the new project, four cores, Protein Production, Structure Analysis, Control of Protein Functions with Compounds, and Informatics, have been established as focus of methodology developments critical for functional and structural studies by the target protein research teams. Within the "Analysis Core" synchrotron radiation plays a pivotal role providing X-ray beams for structural analyses of the target proteins. The two large Japanese synchrotron radiation facilities, SPring-8 and Photon Factory (PF), along with three protein crystallography groups from Hokkaido, Kyoto and Osaka Universities have teamed up to develop two complementary micro-beam beamlines, one on each synchrotron site, and associated technologies for cutting edge structural biology research. At the PF, there are 5 operational beamlines which are equipped with state-of-the-art instrumentation for high-throughput protein crystallography experiments. Within the TPRP framework, the PF is developing a micro-focus beamline optimized for a lower energy single anomalous diffraction (SAD) experiment. This will be particularly useful for structure determination of difficult protein targets for which heavy atom derivatives or selenomethionine substitution does not work and other standard phasing methods fail to give structure solutions. This will augment the capabilities of the PF structural biology beamlines with similar look-and-feel experimental environments.

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  51. Complexity in influenza virus targeted drug design: interaction with human sialidases. 査読有り 国際共著 国際誌

    Leonard M G Chavas, Ryuichi Kato, Nobuhiro Suzuki, Mark von Itzstein, Maretta C Mann, Robin J Thomson, Jeffrey C Dyason, Jennifer McKimm-Breschkin, Paola Fusi, Cristina Tringali, Bruno Venerando, Guido Tettamanti, Eugenio Monti, Soichi Wakatsuki

    Journal of medicinal chemistry   53 巻 ( 7 ) 頁: 2998 - 3002   2010年4月

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    担当区分:筆頭著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:AMER CHEMICAL SOC  

    With the global spread of the pandemic H1N1 and the ongoing pandemic potential of the H5N1 subtype, the influenza virus represents one of the most alarming viruses spreading worldwide. The influenza virus sialidase is an effective drug target, and a number of inhibitors are clinically effective against the virus (zanamivir, oseltamivir, peramivir). Here we report structural and biochemical studies of the human cytosolic sialidase Neu2 with influenza virus sialidase-targeting drugs and related compounds.

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  52. Biophysical and X-ray crystallographic analysis of Mps1 kinase inhibitor complexes. 査読有り 国際共著 国際誌

    Matthew L H Chu, Zhaolei Lang, Leonard M G Chavas, João Neres, Olga S Fedorova, Lydia Tabernero, Mike Cherry, David H Williams, Kenneth T Douglas, Patrick A Eyers

    Biochemistry   49 巻 ( 8 ) 頁: 1689 - 701   2010年3月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:AMER CHEMICAL SOC  

    The dual-specificity protein kinase monopolar spindle 1 (Mps1) is a central component of the mitotic spindle assembly checkpoint (SAC), a sensing mechanism that prevents anaphase until all chromosomes are bioriented on the metaphase plate. Partial depletion of Mps1 protein levels sensitizes transformed, but not untransformed, human cells to therapeutic doses of the anticancer agent Taxol, making it an attractive novel therapeutic cancer target. We have previously determined the X-ray structure of the catalytic domain of human Mps1 in complex with the anthrapyrazolone kinase inhibitor SP600125. In order to validate distinct inhibitors that target this enzyme and improve our understanding of nucleotide binding site architecture, we now report a biophysical and structural evaluation of the Mps1 catalytic domain in the presence of ATP and the aspecific model kinase inhibitor staurosporine. Collective in silico, enzymatic, and fluorescent screens also identified several new lead quinazoline Mps1 inhibitors, including a low-affinity compound termed Compound 4 (Cpd 4), whose interaction with the Mps1 kinase domain was further characterized by X-ray crystallography. A novel biophysical analysis demonstrated that the intrinsic fluorescence of SP600125 changed markedly upon Mps1 binding, allowing spectrophotometric displacement analysis and determination of dissociation constants for ATP-competitive Mps1 inhibitors. By illuminating the structure of the Mps1 ATP-binding site our results provide novel biophysical insights into Mps1-ligand interactions that will be useful for the development of specific Mps1 inhibitors, including those employing a therapeutically validated quinazoline template.

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  53. Fully automated data collection using PAM and the development of PAM/SPACE reversible cassettes 招待有り 査読有り 国際誌

    Masahiko Hiraki, Shokei Watanabe, Leonard M. G. Chavas, Yusuke Yamada, Naohiro Matsugaki, Noriyuki Igarashi, Soichi Wakatsuki, Masahiro Fujihashi, Kunio Miki, Seiki Baba, Go Ueno, Masaki Yamamoto, Mamoru Suzuki, Atsushi Nakagawa, Nobuhisa Watanabe, Isao Tanaka

    AIP Conference Proceedings   1234 巻 ( 1 ) 頁: 673   2010年

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    記述言語:英語   掲載種別:研究論文(国際会議プロシーディングス)   出版者・発行元:AIP Publishing LLC  

    To remotely control and automatically collect data in high-throughput X-ray data collection experiments, the Structural Biology Research Center at the Photon Factory (PF) developed and installed sample exchange robots PAM (PF Automated Mounting system) at PF macromolecular crystallography beamlines; BL-5A, BL-17A, AR-NW12A and AR-NE3A. We developed and installed software that manages the flow of the automated X-ray experiments; sample exchanges, loop-centering and X-ray diffraction data collection. The fully automated data collection function has been available since February 2009. To identify sample cassettes, PAM employs a two-dimensional bar code reader. New beamlines, BL-1A at the Photon Factory and BL32XU at SPring-8, are currently under construction as part of Targeted Proteins Research Program (TPRP) by the Ministry of Education, Culture, Sports, Science and Technology of Japan. However, different robots, PAM and SPACE (SPring-8 Precise Automatic Cryo-sample Exchanger), will be installed at BL-1A and BL32XU, respectively. For the convenience of the users of both facilities, pins and cassettes for PAM and SPACE are developed as part of the TPRP. © 2010 American Institute of Physics.

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  54. エフェクタータンパク質群による Rab27 取り込みへの 構造的知見 招待有り 査読有り

    レオナルド シャバス, 川崎政人, 若槻壮市, 伊原健太郎

    日本結晶学会誌   51 巻   頁: 334 - 339   2009年

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    担当区分:筆頭著者, 責任著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:The Crystallographic Society of Japan  

    小胞輸送の異常によって引き起こされる疾患のいくつかに低分子量 GTPase である Rab の 機能不全が関与することが明らかになってきている. とりわけRab27サブファミリーは, その 機能不全が疾患に直接かかわることから, 小胞輸送における膜のドッキング過程の研究におい てモデル分子として広く利用されている. しかしながら, 構造化学的な知見は乏しく, 数多く 存在する Rab の中で, Rab27 のエフェクタータンパク質はどのようなメカニズムで Rab27 を見 分けているのか, また, Rab27のエフェクタータンパク質は11種類存在するが, それらの間で どのような違いでもってRab27と相互作用を行っているかについでは, いまだ不明である. そ こで, Rab27 サブファミリーによって制御される輸送小胞の膜融合過程の分子基盤を明らかに するために, Rab単体, およびエフェクタータンパク質であるSlp2-aとの複合体のX線結晶構 造解析を行った.

    DOI: 10.5940/jcrsj.51.334

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  55. Elucidation of Rab27 recruitment by its effectors: structure of Rab27a bound to Exophilin4/Slp2-a 査読有り 国際誌

    Leonard M G Chavas, Kentaro Ihara, Masato Kawasaki, Seiji Torii, Tamami Uejima, Ryuichi Kato, Tetsuro Izumi, Soichi Wakatsuki

    Structure (London, England : 1993)   16 巻 ( 10 ) 頁: 1468 - 77   2008年10月

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    担当区分:筆頭著者, 責任著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:CELL PRESS  

    Rab GTPases coordinate vesicular trafficking within eukaryotic cells by collaborating with a set of effector proteins. Rab27a regulates numerous exocytotic pathways, and its dysfunction causes the Griscelli syndrome human immunodeficiency. Exophilin4/Slp2-a localizes on phosphatidylserine-enriched plasma membrane, and its N-terminal Rab27-binding domain (RBD27) specifically recognizes Rab27 on the surfaces of melanosomes and secretory granules prior to docking and fusion. To characterize the selective binding of Rab27 to 11 various effectors, we have determined the 1.8 A resolution structure of Rab27a in complex with Exophilin4 RBD27. The effector packs against the switch and interswitch elements of Rab27a, and specific affinity toward Rab27a is modulated by a shift in the orientation of the effector structural motif (S/T)(G/L)xW(F/Y)(2). The observed structural complementation between the interacting surfaces of Rab27a and Exophilin4 sheds light on the disparities among the Rab27 effectors and outlines a general mechanism for their recruitment.

    DOI: 10.1016/j.str.2008.07.015

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  56. Crystal structure of the catalytic domain of the mitotic checkpoint kinase Mps1 in complex with SP600125 査読有り 国際誌

    Matthew L H Chu, Leonard M G Chavas, Kenneth T Douglas, Patrick A Eyers, Lydia Tabernero

    The Journal of biological chemistry   283 巻 ( 31 ) 頁: 21495 - 500   2008年8月

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    担当区分:筆頭著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC  

    Chromosomal instability can result from defective control of checkpoints and is associated with malignant cell growth. Monopolar spindle 1 (Mps1) is a dual-specificity protein kinase that has important roles in the prevention of aneuploidy during the cell cycle and might therefore be a potential target for new therapeutic agents in the treatment of cancer. To gain insights into the molecular mechanism of Mps1 inhibition by small molecules, we determined the x-ray structure of Mps1, both alone and in complex with the ATP-competitive inhibitor SP600125. Mps1 adopts a classic protein kinase fold, with the inhibitor sitting in the ATP-binding site where it is stabilized by hydrophobic interactions. We identified a secondary pocket, not utilized by SP600125, which might be exploited for the rational design of specific Mps1 inhibitors. These structures provide important insights into the interaction of this protein kinase with small molecules and suggest potential mechanisms for Mps1 regulation.

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  57. Purification, crystallization and preliminary X-ray crystallographic analysis of Rab27a GTPase in complex with exophilin4/Slp2-a effector 査読有り 国際誌

    Leonard M G Chavas, Kentaro Ihara, Masato Kawasaki, Ryuichi Kato, Tetsuro Izumi, Soichi Wakatsuki

    Acta crystallographica. Section F, Structural biology and crystallization communications   64 巻 ( Pt 7 ) 頁: 599 - 601   2008年7月

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    担当区分:筆頭著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    By switching between GTP-active and GDP-inactive conformations, small Ras GTPases partly regulate membrane trafficking, cell growth and cytoskeleton dynamics. Among Rab GTPases, the Rab27 subfamily, which comprises Rab27a and Rab27b, controls the proper targeting of secretory vesicles to the plasma membrane. GppNHp-bound Rab27a in complex with the Rab27-binding domain of exophilin4/Slp2-a effector has been purified and crystallized for structural studies. The crystals belong to space group P2(1)2(1)2(1) and a complete data set was collected to a resolution of 1.8 A. Eventually, the structural characterization of the Rab27a-exophilin4/Slp2-a complex will clarify Rab27 recognition by its effectors prior to vesicle tethering and docking.

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  58. Atomic model of Rab27a: Exophilin4/Slp2-a complex: Structural studies on vesicular transport 査読有り 国際誌

    Leonard M. G. Chavas, Kentaro Ihara, Masato Kawasaki, Ryuichi Kato, Tetsuro Izumi, Soichi Wakatsuki

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   64 巻   頁: C333 - C333   2008年

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    担当区分:筆頭著者   記述言語:英語   掲載種別:研究論文(研究会,シンポジウム資料等)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Atomic model of Rab27a: Exophilin4/Slp2-a complex: Structural studies on vesicular transport

    DOI: 10.1107/S0108767308089344

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  59. Structure of the small GTPase Rab27b shows an unexpected swapped dimer. 査読有り 国際誌

    Leonard M G Chavas, Seiji Torii, Hironari Kamikubo, Masato Kawasaki, Kentaro Ihara, Ryuichi Kato, Mikio Kataoka, Tetsuro Izumi, Soichi Wakatsuki

    Acta crystallographica. Section D, Biological crystallography   63 巻 ( Pt 7 ) 頁: 769 - 79   2007年7月

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    担当区分:筆頭著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Members of the Rab family of small GTPases regulate membrane traffic within the cell by recruiting their specific effectors in a nucleotide-dependent manner. The Rab27 subfamily consists of Rab27a and Rab27b, which share 70% sequence identity. By interacting with a large set of effector proteins such as melanophilin and granuphilin, both Rab27a and Rab27b regulate the exocytosis of secretory lysosomes. Here, the crystal structures of mouse Rab27b in complex with GDP have been determined in three distinct crystal lattices. Surprisingly, Rab27b-GDP exists in an open conformation with protruding switch and interswitch regions, which are stabilized through dimerization by means of domain-swapping in the crystals. In contrast, small-angle X-ray scattering measurements showed an extended monomer form of Rab27b in solution. The observed dimer formation of Rab27b-GDP in the crystals would restrain the highly flexible switch regions. Possible biological implications of this atypical structure of Rab27b and its plausible influence in effector interaction are discussed.

    DOI: 10.1107/S0907444907019725

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  60. Development of an automated large-scale protein-crystallization and monitoring system for high-throughput protein-structure analyses. 査読有り 国際誌

    Masahiko Hiraki, Ryuichi Kato, Minoru Nagai, Tadashi Satoh, Satoshi Hirano, Kentaro Ihara, Norio Kudo, Masamichi Nagae, Masanori Kobayashi, Michio Inoue, Tamami Uejima, Shunichiro Oda, Leonard M G Chavas, Masato Akutsu, Yusuke Yamada, Masato Kawasaki, Naohiro Matsugaki, Noriyuki Igarashi, Mamoru Suzuki, Soichi Wakatsuki

    Acta crystallographica. Section D, Biological crystallography   62 巻 ( Pt 9 ) 頁: 1058 - 65   2006年9月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:INT UNION CRYSTALLOGRAPHY  

    Protein crystallization remains one of the bottlenecks in crystallographic analysis of macromolecules. An automated large-scale protein-crystallization system named PXS has been developed consisting of the following subsystems, which proceed in parallel under unified control software: dispensing precipitants and protein solutions, sealing crystallization plates, carrying robot, incubators, observation system and image-storage server. A sitting-drop crystallization plate specialized for PXS has also been designed and developed. PXS can set up 7680 drops for vapour diffusion per hour, which includes time for replenishing supplies such as disposable tips and crystallization plates. Images of the crystallization drops are automatically recorded according to a preprogrammed schedule and can be viewed by users remotely using web-based browser software. A number of protein crystals were successfully produced and several protein structures could be determined directly from crystals grown by PXS. In other cases, X-ray quality crystals were obtained by further optimization by manual screening based on the conditions found by PXS.

    DOI: 10.1107/S0907444906023821

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  61. Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition. 査読有り 国際誌

    Leonard M G Chavas, Cristina Tringali, Paola Fusi, Bruno Venerando, Guido Tettamanti, Ryuichi Kato, Eugenio Monti, Soichi Wakatsuki

    The Journal of biological chemistry   280 巻 ( 1 ) 頁: 469 - 75   2005年1月

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    担当区分:筆頭著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:American Society for Biochemistry and Molecular Biology, Inc.  

    Gangliosides play key roles in cell differentiation, cell-cell interactions, and transmembrane signaling. Sialidases hydrolyze sialic acids to produce asialo compounds, which is the first step of degradation processes of glycoproteins and gangliosides. Sialidase involvement has been implicated in some lysosomal storage disorders such as sialidosis and galactosialidosis. Neu2 is a recently identified human cytosolic sialidase. Here we report the first high resolution x-ray structures of mammalian sialidase, human Neu2, in its apo form and in complex with an inhibitor, 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (DANA). The structure shows the canonical six-blade beta-propeller observed in viral and bacterial sialidases with its active site in a shallow crevice. In the complex structure, the inhibitor lies in the catalytic crevice surrounded by ten amino acids. In particular, the arginine triad, conserved among sialidases, aids in the proper positioning of the carboxylate group of DANA within the active site region. The tyrosine residue, Tyr(334), conserved among mammalian and bacterial sialidases as well as in viral neuraminidases, facilitates the enzymatic reaction by stabilizing a putative carbonium ion in the transition state. The loops containing Glu(111) and the catalytic aspartate Asp(46) are disordered in the apo form but upon binding of DANA become ordered to adopt two short alpha-helices to cover the inhibitor, illustrating the dynamic nature of substrate recognition. The N-acetyl and glycerol moieties of DANA are recognized by Neu2 residues not shared by bacterial sialidases and viral neuraminidases, which can be regarded as a key structural difference for potential drug design against bacteria, influenza, and other viruses.

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MISC 4

  1. Macromolecular structures from nanocrystals 招待有り

    Chavas L.M.G.H  

    Energy Recover Linac - Conceptual Design Report   2012年10月

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    担当区分:筆頭著者, 最終著者, 責任著者   記述言語:英語   掲載種別:機関テクニカルレポート,技術報告書,プレプリント等  

  2. Cover Picture: The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed 招待有り 査読有り 国際共著 国際誌

    Larissa Dirr, Dr. Ibrahim M. El-Deeb, Dr. Patrice Guillon, Cindy J. Carroux, Dr. Leonard M. G. Chavas, Prof. Mark von Itzstein  

    Angewandte Chemie (International ed. in English)54 巻 ( 10 ) 頁: Cover   2015年2月

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    記述言語:英語  

    The human parainfluenza virus type 3 (hPIV-3) is one of the leading causes of lower respiratory tract disease in children. In their Communication on page 2936 ff., M. von Itzstein, I. M. El-Deeb, P. Guillon, L. M. G. Chavas, and co-workers investigate the catalytic mechanism of hPIV-3 haemagglutinin-neuraminidase (HN) and determine that it is a retaining glycohydrolase. Moreover hPIV-3 HN utilizes a highly conserved tyrosine residue to form a transient covalent bond with the anomeric carbon of the substrate. Finally a novel sialic acid derivative showed potency in virus blockade assays.

    DOI: 10.1002/anie.201500511

  3. Cover Picture : Structural Insights into Rab27 Recruitment by its Effectors 招待有り 査読有り

    Leonard M. G. CHAVAS, Kentaro IHARA, Masato KAWASAKI, Soichi WAKATSUKI  

    日本結晶学会誌51 巻 ( 6 ) 頁: Cover   2010年12月

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    担当区分:筆頭著者, 責任著者   記述言語:英語  

    DOI: https://doi.org/10.5940/jcrsj.51.Cover06

  4. Cover Picture : Structure of the human mitotic checkpoint kinase Mps1 catalytic domain apo form and inhibitor SP600125-bound form 招待有り 査読有り 国際共著

    Matthew L. H. Chu, Leonard M. G. Chavas, Kenneth T. Douglas, Patrick A. Eyers, Lydia Tabernero  

    J. Biol. Chem.283 巻 ( 31 ) 頁: Cover   2008年8月

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    担当区分:筆頭著者   記述言語:英語  

    DOI: 10.1074/jbc.M803026200

講演・口頭発表等 12

  1. Laying the groundwork of an in vivo macromolecular crystallography platform at Synchrotron SOLEIL 招待有り 国際共著 国際会議

    Chavas

    14th International Conference on Synchrotron Radiation Instrumentation  2022年3月30日 

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    開催年月日: 2022年3月 - 2022年4月

    記述言語:英語   会議種別:口頭発表(招待・特別)  

    国名:ドイツ連邦共和国  

    細胞や生体内に自然に存在するタンパク質結晶の同定は、in vivo MXと呼ばれる新しいタイプの高分子結晶学(MX)と構造生物学の窓を開くものである。過去10年間、試料の取り扱いや運搬方法をさらに開発し、これらの技術を容易に入手できるin vivo MXシステムの構造決定や解析に応用することで、in vivo結晶成長を規定するまだ制御できない事象について、より深い洞察を得るための努力が払われてきた。
     より多くの人々がivMXを利用できるようにするため、シンクロトロンSOLEIL(フランス)で完全なパイプラインの実装に向けたマイルストーンが設定された。本発表では、ivMXの仕組み、プラットフォームの背後にある基礎知識、そしてこの魅力的な自然現象に関わる事象の完全な特徴付けを試みる中で得られた有望な結果について紹介する予定である。

    DOI: 10.5281/zenodo.6403801

  2. Evolutions in Synchrotron based integrated structural biology at SOLEIL 国際共著 国際会議

    A. Thompson and L.M.G. Chavas

    XXV IUCr Congress  2021年8月18日 

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    開催年月日: 2021年8月

    記述言語:英語   会議種別:口頭発表(一般)  

  3. VISION FOR AN INTEGRATED STRUCTURAL BIOLOGY AND METHODOLOGY

    Chavas Leo

    2021年3月30日 

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    開催年月日: 2021年3月

    記述言語:英語   会議種別:口頭発表(一般)  

    開催地:Nagoya University   国名:日本国  

    DOI: 10.5281/zenodo.4646448

  4. VISION FOR AN INTEGRATED STRUCTURAL BIOLOGY AND METHODOLOGY

    シンクロトロン光センターシンポジウム  2021年3月30日  シンクロトロン光センター

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    記述言語:英語   会議種別:口頭発表(一般)  

    国名:日本国  

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    その他リンク: https://doi.org/10.5281/zenodo.4646448

  5. Combining expert methods for multi-scale and correlated analysis 招待有り 国際会議

    2021年12月3日 

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    記述言語:英語   会議種別:口頭発表(一般)  

    国名:フランス共和国  

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  6. High-pressure macromolecular crystallography at Aichi-SR

    第62回高圧討論会 

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    記述言語:日本語   会議種別:ポスター発表  

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  7. In vivo Macromolecular Crystallography 招待有り

    シャバス レオナルド

    日本結晶学会2021  2021年11月21日 

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    記述言語:日本語   会議種別:口頭発表(一般)  

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  8. MICROFLUIDICS-BASED STRATEGIES FOR SERIAL PROTEIN CRYSTALLOGRAPHY AT SYNCHROTRON FACILITIES

    2021年11月29日 

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    記述言語:英語   会議種別:ポスター発表  

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  9. NEWS FROM PROXIMA1 & PROXIMA2A @ SYNCHROTRON SOLEIL

    2021年11月29日 

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    記述言語:英語   会議種別:ポスター発表  

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  10. STRUCTURAL AND FUNCTIONAL STUDY OF THE COMPLEX FORMED BY THE WERNER PROTEIN (WRN) AND THE KU70/KU80 HETERODIMER 招待有り

    2021年11月30日 

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    記述言語:英語   会議種別:ポスター発表  

    国名:フランス共和国  

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  11. The Synchrotron Radiation Research Center at Nagoya University

    日本放射光学会  2022年1月8日 

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    記述言語:日本語   会議種別:口頭発表(一般)  

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  12. 名古屋大学ASBiM研究グループによる統合生物学的な研究紹介

    2021年10月4日 

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    記述言語:日本語   会議種別:公開講演,セミナー,チュートリアル,講習,講義等  

    生物の複雑で相互作用する現象を、マクロからミクロの視点で理解し、化学反応として解釈することは、生命科学の大きな挑戦である。それには、スケールにあった手法を用いて、生体高分子の構造、細胞内の相互作用、生物個体の応答まで、階層的な研究に取り組む必要がある。現代の生物学では、これら複数の科学情報を共用する研究プラットフォームの導入が求められている。本公演では、応用構造生物学と方法論開発を掲げる当研究グループによる、統合生物学としての可能性の1つである、細胞内で天然タンパク質を結晶化させる斬新な技法をハイライトとして紹介する。

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Works(作品等) 6

  1. Artwork illustration for press release on methane emission

    Chavas L.

    2022年3月

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    作品分類:芸術活動  

    メタン排出に関する作業を説明するためのアートワーク。

  2. Artwork illustration for press release on black rot disease

    Chavas L.

    2021年12月

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    作品分類:芸術活動  

    黒色ロート製薬で行われた作業を説明するためのアートワーク。

  3. Website development (ASBiM group)

    Chavas L.

    2021年4月
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    2022年3月

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    作品分類:Web Service  

    研究グループASBiMのホームとリンクされたインターネットページの開発と維持管理

  4. Website development (BL2S1 beamline)

    Chavas L.

    2021年4月
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    2022年3月

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    作品分類:Web Service  

    シンクロトロンAichiSRの研究装置BL2S1のHomeとLinkedのインターネットページの開発と維持管理

  5. ビームライン制御のためのソフトウェア開発(UGUI2)

    Joint research group - Photon Factory SBRC

    2022年4月
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    現在

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    作品分類:ソフトウェア   発表場所:愛知SRの名古屋大学BL2S1  

    UGUI2は、フォトンファクトリーの構造生物学用ビームラインで行われる実験を制御するために開発されたソフトウェアです。このソフトウェアを改良し、AichiSRの名古屋大学BL2S1ビームラインで実装した。

  6. Website development (NUSR Symposium 2021)

    Chavas L.

    2021年9月
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    2022年3月

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    作品分類:Web Service  

    主催するNUSRシンポジウム2021のHomeとLinkedのインターネットページの開発・維持管理

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その他研究活動 10

  1. hNeu2タンパク質の研究のコーディネート

    2022年4月
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    hNeu2タンパク質に関連するプロジェクトのコーディネート。
    - 中島 武琉 (M1学生):実験プロトコルの作成
    - 小野田 (助教授):実験補助

  2. マイクロ流体の研究のコーディネート

    2022年4月
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    マイクロ流体工学に関連するプロジェクトの調整:
    - 1つの日本のコラボレーション(Ass.Prof. Matsugaki)
    - 1つのフランスのコラボレーション(Dr. Vasireddi)

  3. Ferritinタンパク質の研究のコーディネート

    2022年4月
    -
    現在

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    Ferritinタンパク質に関連するプロジェクトのコーディネート。
    - 河野 友祐 (M1学生):実験プロトコルの作成
    - 小野田 (助教授):実験補助

  4. 愛知SRにおける名古屋大学BL2S1ビームラインの運用・維持・高度化への貢献

    2022年4月
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  5. 研究内容の調整、生体分子物理学グループとの連携

    2022年4月
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    生体分子物理学グループとの連携調整。
    - 毎週90分のミーティングを開催する。
    - 全メンバーとの30分程度のディスカッションを隔週で行う。

  6. フランスとの国際共同研究プログラム立ち上げ

    2022年4月
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    フランスの大学との国際的な共同研究の立ち上げに取り組む。
    - 在日フランス大使館の学術研究担当者と可能性について協議する。

  7. あいちSRのビームラインの運営、整備、高度化への貢献

    2021年4月
    -
    2022年3月

     詳細を見る

    あいちSRのビームラインの運営、整備、高度化への貢献

  8. あいちSR職員等への教育、技術指導、あいちSRでのビームライン担当者ミーティング主催などを通じたあいちSR運営への貢献

    2021年4月
    -
    2022年3月

     詳細を見る

    あいちSR職員等への教育、技術指導、あいちSRでのビームライン担当者ミーティング主催などを通じたあいちSR運営への貢献

  9. あいちSRを利用する学生への教育指導

    2021年4月
    -
    2022年3月

     詳細を見る

    あいちSRを利用する学生への教育指導

  10. あいちSRを利用する名古屋大学教職員並びに学生の支援

    2021年4月
    -
    2022年3月

     詳細を見る

    あいちSRを利用する名古屋大学教職員並びに学生の支援

▼全件表示

科研費 1

  1. 高分子結晶学における紫外線の研究

    研究課題/研究課題番号:22770161  2010年 - 2011年

    シャバス レオナルド

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    担当区分:研究代表者 

    配分額:3900000円 ( 直接経費:3000000円 、 間接経費:900000円 )

    生体高分子結晶の構造決定にUV放射光を有効に利用することがこの研究の最終目標である。UV放射誘起フェージング(UV-RIP)のための一般的な方法論を開発する目的で、タンパク質モデルへのUV放射の具体的な効果が調べられた。高分子結晶を強いUV光に曝すと顕著なダメージにより低い電子密度となる。UV照射された結晶で観測される特定のダメージを結晶構造決定に最大限に活用するために、UV-RIPについての一般的方法論と半自動データ解析ソフトウェアが実装された。

 

担当経験のある科目 (本学) 2

  1. 物理工学セミナー

    2021

     詳細を見る

    生体分子の物理

  2. 生体分子の物理セミナー

    2021

     詳細を見る

    統合生物学におけるin vivo結晶学の可能性の説明

担当経験のある科目 (本学以外) 4

  1. あいちSRのビームラインの運営、整備、高度化への貢献

    2021年4月 - 2022年3月 あいちSR)

     詳細を見る

    科目区分:その他  国名:日本国

  2. あいちSRを利用する名古屋大学教職員並びに学生の支援

    2021年4月 - 2022年3月 あいちSR)

     詳細を見る

    科目区分:その他  国名:日本国

  3. あいちSRを利用する学生への教育指導

    2021年4月 - 2022年3月 あいちSR)

     詳細を見る

    科目区分:その他  国名:日本国

  4. あいちSR職員等への教育、技術指導、あいちSRでのビームライン担当者ミーティング主催などを通じたあいちSR運営への貢献

    2021年4月 - 2022年3月 あいちSR)

     詳細を見る

    科目区分:その他  国名:日本国

 

社会貢献活動 12

  1. ASBiMサマースクール2021

    役割:司会, 講師, 実演, 寄稿

    ASBiMサマースクール2021  2021年8月

  2. 名大博物館 タンパク質結晶のイベント

    役割:パネリスト, 司会, 講師, 助言・指導, 実演, 寄稿

    名大博物館  名大博物館 タンパク質結晶のイベント  2021年8月

  3. 専用プロモーションビデオの設置で名古屋大学BL2S1の活用をPR

    役割:講師, 助言・指導, 実演, 調査担当, 報告書執筆, 寄稿

    ASBiM group  BL2S1プロモーションビデオ  AichiSR  2022年4月 - 現在

     詳細を見る

    対象: 高校生, 大学生, 大学院生, 教育関係者, 保護者, 研究者, 社会人・一般, 学術団体, 企業, 市民団体, 行政機関, メディア

    種別:会誌・広報誌

    名古屋大学BL2S1ビームラインにおける様々な活動を、プロモーションビデオの設定により説明。

  4. 名大のパンフレットにAichiSRの活用をPR

    役割:実演

    名古屋大学工学部  Meidaism  AichiSR  2022年4月

     詳細を見る

    対象: 高校生, 大学生, 大学院生, 教育関係者, 保護者, 研究者, 社会人・一般, 学術団体, 企業, 市民団体, 行政機関, メディア

    種別:会誌・広報誌

    名古屋大学工学部における様々な活動の説明

  5. BL2S1ビームラインの一般公開について

    役割:助言・指導, 情報提供

    中部イノベネット  2022年4月 - 現在

     詳細を見る

    対象: 企業, メディア

    種別:セミナー・ワークショップ

    愛知SRの名古屋大学BL2S1ビームラインの利用促進を目的としたセミナーを開催する。

  6. How a particular protein regulates up to two-thirds of the world's methane emission: key mechanism for methane emission in anaerobic environments is now understood, potentially helping the fight against climate change

    役割:報告書執筆

    Nagoya University press release  2022年3月

  7. ゴキブリミルク:持続可能な食料源

    役割:講師

    アリアンス・フランセーズ愛知フランス協会  ASFAミーティング・講演会  2022年1月

  8. Hope rising for understanding and protecting against black rot disease

    役割:調査担当, 報告書執筆

    Nagoya University press release  2021年12月

  9. ASBiMセミナーシリーズ、3回位目

    役割:司会, インタビュアー

    ASBiMセミナーシリーズ  2021年11月

  10. 名古屋大学ASBIM研究グループによる統合 生物学的な研究紹介

    役割:講師

    基盤医学特論  基盤医学特論 開講通知   2021年10月

  11. ASBiMセミナーシリーズ、2回位目

    役割:司会, インタビュアー

    ASBiMセミナーシリーズ  2021年7月

  12. ASBiMセミナーシリーズ、1回位目

    役割:司会, インタビュアー

    ASBiMセミナーシリーズ  2021年7月

▼全件表示

学術貢献活動 13

  1. 日本結晶学会年会2024 国際学術貢献

    役割:企画立案・運営等, 監修

    日本結晶学会  2022年1月 - 2022年3月

     詳細を見る

    種別:大会・シンポジウム等 

  2. メソスケールのイメージング手法として、軟X線顕微鏡(SXTM) 国際学術貢献

    役割:パネル司会・セッションチェア等

    第95回日本生化学会大会公  2022年1月 - 2022年3月

     詳細を見る

    種別:大会・シンポジウム等 

  3. 科学雑誌の査読(改訂原稿:nw5113) 国際学術貢献

    役割:査読

    Scientific journal : Acta Crystallographica Section F: Structural Biology Communications  2022年4月

     詳細を見る

    種別:査読等 

  4. 第10回あいちシンクロトロン光センター事業成果発表会

    AichiSR  ( AichiSR ) 2022年4月

     詳細を見る

    種別:大会・シンポジウム等 

    第10回あいちシンクロトロン光センター事業成果発表会に参加。

  5. 生体分子物理学研究会第3回会合の開催について

    役割:企画立案・運営等, 監修, 学術調査立案・実施

    シャバス レオナルド  ( Nagoya University 3rd building ) 2022年4月

     詳細を見る

    種別:学会・研究会等 

    生体分子物理学グループ内の組織について議論するための冗長な会議。
    ミーティング#3:小野田教授によるプレゼンテーション

  6. 名古屋大学工学部委員会第1回会議への参加

    役割:学術調査立案・実施

    名古屋大学工学部  ( Nagoya University ES Hall ) 2022年4月

     詳細を見る

    名古屋大学工学部内の組織について話し合う冗長な会議

  7. 生体分子物理学研究会第2回会合の開催について

    役割:企画立案・運営等, 監修, 学術調査立案・実施

    シャバス レオナルド  ( Nagoya University 3rd building ) 2022年4月

     詳細を見る

    種別:学会・研究会等 

    生体分子物理学グループ内の組織について議論するための冗長な会議。
    ミーティング#2:梅名教授によるプレゼンテーション

  8. 生体分子物理学研究会第1回会合の開催について

    役割:企画立案・運営等, 監修, 学術調査立案・実施

    シャバス レオナルド  ( Nagoya University 3rd building ) 2022年4月

     詳細を見る

    種別:学会・研究会等 

    生体分子物理学グループ内の組織について議論するための冗長な会議。

  9. NUSR シンポジウム 2021 国際学術貢献

    役割:企画立案・運営等, 監修

    2022年1月

     詳細を見る

    種別:大会・シンポジウム等 

  10. 科学期刊审查(手稿 : LC-ART-05-2021-000417) 国際学術貢献

    役割:査読

    Scientific journal : Lab on a Chip 

     詳細を見る

    種別:査読等 

  11. 科学期刊审查(手稿 : nw5113) 国際学術貢献

    役割:査読

    Scientific journal : Acta Crystallographica Section F: Structural Biology Communications 

     詳細を見る

    種別:査読等 

  12. 科学期刊审查(手稿 : BIOPHYSCHEM-D-21-00204) 国際学術貢献

    役割:査読

    Scientific journal : Biophysical Chemistry 

     詳細を見る

    種別:査読等 

  13. 科学期刊审查(手稿 : JM-2021-01612W) 国際学術貢献

    役割:査読

    Scientific journal : Journal of Medicinal Chemistry 

     詳細を見る

    種別:査読等 

▼全件表示