| Literature DB >> 22653729 |
Sébastien Boutet1, 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 Hart, Jack 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.
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 (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.Entities:
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Year: 2012 PMID： 22653729 PMCID： PMC3788707 DOI： 10.1126/science.1217737
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728