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  Femtosecond X-ray protein nanocrystallography

Chapman, H. N., Fromme, P., Barty, A., White, T. A., Kirian, R. A., Aquila, A., et al. (2011). Femtosecond X-ray protein nanocrystallography. Nature, 470(7332), 73-77. doi:10.1038/nature09750.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-0AD7-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-0AD8-8
Genre: Journal Article
Alternative Title : Femtosecond X-ray protein nanocrystallography

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Chapman, Henry N., Author
Fromme, Petra, Author
Barty, Anton, Author
White, Thomas A., Author
Kirian, Richard A., Author
Aquila, Andrew, Author
Hunter, Mark S., Author
Schulz, Joachim, Author
DePonte, Daniel P., Author
Weierstall, Uwe, Author
Doak, R. Bruce1, Author              
Filipe R. N. C. Maia, Filipe R. N. C., Author
Martin, Andrew V., Author
Schlichting, Ilme1, Author              
Lomb, Lukas1, Author              
Coppola, Nicola, Author
Shoeman, Robert L.1, Author              
Epp, Sascha W., Author
Hartmann, Robert, Author
Rolles, Daniel1, Author              
Rudenko, Artem, AuthorFoucar, Lutz1, Author              Kimmel, Nils, AuthorWeidenspointner, Georg, AuthorHoll, Peter, AuthorLiang, Mengning, AuthorBarthelmess, Miriam, AuthorCaleman, Carl, AuthorBoutet, Sébastien, AuthorBogan, Michael J., AuthorKrzywinski, Jacek, AuthorBostedt, Christoph, AuthorBajt, Saša, AuthorGumprecht, Lars, AuthorRudek, Benedikt1, Author              Erk, Benjamin1, Author              Schmidt, Carlo, AuthorHömke, André, AuthorReich, Christian, AuthorPietschner, Daniel, AuthorStrüder, Lothar, AuthorHauser, Günter, AuthorGorke, Hubert, AuthorUllrich, Joachim, AuthorHerrmann, Sven, AuthorSchaller, Gerhard, AuthorSchopper, Florian, AuthorSoltau, Heike, AuthorKühnel, Kai−Uwe, AuthorMesserschmidt, Marc, AuthorBozek, John D., AuthorHau−Riege, Stefan P., AuthorFrank, Matthias, AuthorHampton, Christina Y., AuthorSierra, Raymond G., AuthorStarodub, Dmitri, AuthorWilliams,, Garth J., AuthorHajdu, Janos, AuthorTimneanu, Nicusor, AuthorSeibert, M. Marvin, AuthorAndreasson, Jakob, AuthorRocker, Andrea1, Author              Jönsson, Olof, AuthorSvenda, Martin, AuthorStern, Stephan, AuthorNass, Karol1, Author              Andritschke, Robert, AuthorSchroeter, Claus−Dieter, AuthorKrasniqi, Faton1, Author              Bott, Mario1, Author              Schmidt, Kevin E., AuthorWang, Xiaoyu, AuthorGrotjohann, Ingo, AuthorHolton, James M., AuthorBarends, Thomas1, Author              Neutze, Richard, AuthorMarchesini, Stefano, AuthorFromme, Raimund, AuthorSchorb, Sebastian, AuthorRupp, Daniela, AuthorAdolph, Marcus, AuthorGorkhover, Tais, AuthorAndersson, Inger, AuthorHirsemann, Helmut, AuthorPotdevin, Guillaume, AuthorGraafsma, Heinz, AuthorNilsson, Björn, AuthorSpence, John C. H., Author more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded1, 2, 3. It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been determined despite their importance in all living cells. Here we present a method for structure determination where single-crystal X-ray diffraction ‘snapshots' are collected from a fully hydrated stream of nanocrystals using femtosecond pulses from a hard-X-ray free-electron laser, the Linac Coherent Light Source4. We prove this concept with nanocrystals of photosystem I, one of the largest membrane protein complexes5. More than 3,000,000 diffraction patterns were collected in this study, and a three-dimensional data set was assembled from individual photosystem I nanocrystals (˜200?nm to 2?μm in size). We mitigate the problem of radiation damage in crystallography by using pulses briefer than the timescale of most damage processes6. This offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage

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Language(s): eng - English
 Dates: 2010-07-242010-12-092011-02-022011-02-03
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664463
DOI: 10.1038/nature09750
Other: 7738
 Degree: -

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Title: Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 470 (7332) Sequence Number: - Start / End Page: 73 - 77 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238