High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

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

*Corresponding author for this work
417 Citations (Scopus)


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 (less than 1 micrometer by 1 micrometer by 3 micrometers) 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.

Original languageEnglish
Issue number6092
Pages (from-to)362-364
Number of pages3
Publication statusPublished - 20.07.2012


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