High-resolution protein structure determination by serial femtosecond 
crystallography

Boutet, Sébastien; Lomb, Lukas; Williams, Garth J.; Barends, Thomas; Aquila, Andrew; Doak, R. Bruce; Weierstall, Uwe; DePonte, Daniel P.; Steinbrener, Jan; Shoeman, Robert L.; Messerschmidt, Marc; Barty, Anton; White, Thomas A.; Kassemeyer, Stephan; Kirian, Richard A.; Seibert, M. Marvin; Montanez, Paul A.; Kenney, Chris; Herbst, Ryan; Hart, Philip; Pines, Jack; Haller, Gunther; Gruner, Sol M.; Philipp, Hugh T.; Tate, Mark W.; Hromalik, Marianne; Koerner, Lucas J.; van Bakel, Niels; Morse, John; Ghonsalves, Wilfred; Arnlund, David; Bogan, Michael J.; Caleman, Carl; Fromme, Raimund; Hampton, Christina Y.; Hunter, Mark S.; Johansson, Linda; Katona, Gergely; Kupitz, Christopher; Liang, Mengning; Martin, Andrew V.; Nass, Karol; Redecke, Lars; Stellato, Francesco; Timneanu, Nicusor; Wang, Dingjie; Zatsepin, Nadia A. A.; Schafer, Donald; Defever, James; Neutze, Richard; Fromme, Petra; Spence, John C. H.; Chapman, Henry N.; Schlichting, Ilme

doi:10.1126/science.1217737

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High-resolution protein structure determination by serial femtosecond crystallography

MPG-Autoren

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Lomb, Lukas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Barends, Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Doak, R. Bruce
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Steinbrener, Jan
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Shoeman, Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Kassemeyer, Stephan
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Nass, Karol
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting, Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

http://dx.doi.org/10.1126/science.1217737
(beliebiger Volltext)

http://www.sciencemag.org/content/early/2012/05/30/science.1217737.full.pdf
(beliebiger Volltext)

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Zitation

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.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-4927-9

Zusammenfassung

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