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  High-resolution protein structure determination by serial femtosecond crystallography

Boutet, S., Lomb, L., Williams, G. J., Barends, T., Aquila, A., Doak, R. B., et al. (2012). High-resolution protein structure determination by serial femtosecond crystallography. Science, 337(6092), 362-364. doi:10.1126/science.1217737.

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Genre: Journal Article
Alternative Title : High-resolution protein structure determination by serial femtosecond crystallography

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Boutet, Sébastien, Author
Lomb, Lukas1, Author              
Williams, Garth J., Author
Barends, Thomas1, Author              
Aquila, Andrew, Author
Doak, R. Bruce1, Author              
Weierstall, Uwe, Author
DePonte, Daniel P., Author
Steinbrener, Jan1, Author              
Shoeman, Robert L.1, Author              
Messerschmidt, Marc, Author
Barty, Anton, Author
White, Thomas A., Author
Kassemeyer, Stephan1, Author              
Kirian, Richard A., Author
Seibert, M. Marvin, Author
Montanez, Paul A., Author
Kenney, Chris, Author
Herbst, Ryan, Author
Hart, Philip, Author
Pines, Jack, AuthorHaller, Gunther, AuthorGruner, Sol M., AuthorPhilipp, Hugh T., AuthorTate, Mark W., AuthorHromalik, Marianne, AuthorKoerner, Lucas J., Authorvan Bakel, Niels, AuthorMorse, John, AuthorGhonsalves, Wilfred, AuthorArnlund, David, AuthorBogan, Michael J., AuthorCaleman, Carl, AuthorFromme, Raimund, AuthorHampton, Christina Y., AuthorHunter, Mark S., AuthorJohansson, Linda, AuthorKatona, Gergely, AuthorKupitz, Christopher, AuthorLiang, Mengning, AuthorMartin, Andrew V., AuthorNass, Karol1, Author              Redecke, Lars, AuthorStellato, Francesco, AuthorTimneanu, Nicusor, AuthorWang, Dingjie, AuthorZatsepin, Nadia A. A., AuthorSchafer, Donald, AuthorDefever, James, AuthorNeutze, Richard, AuthorFromme, Petra, AuthorSpence, John C. H., AuthorChapman, Henry N., AuthorSchlichting, Ilme1, Author               more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (<1×1×3 μm(3)) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules

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Language(s): eng - English
 Dates: 2011-06-122012-05-212012-05-312012-07-20
 Publication Status: Published in print
 Pages: 3
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 Table of Contents: -
 Rev. Type: Peer
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Title: Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 337 (6092) Sequence Number: - Start / End Page: 362 - 364 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1