Portal de Periódicos da CAPES

High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

2012; American Association for the Advancement of Science; Volume: 337; Issue: 6092 Linguagem: Inglês

10.1126/science.1217737

1095-9203

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, M. Messerschmidt, Anton Barty, Thomas A. White, Stephan Kassemeyer, Richard A. Kirian, M. Seibert, P. Montanez, C. Kenney, Ryan Herbst, Philip Hart, J. Pines, G. Haller, Sol M. Grüner, Hugh T. Philipp, Mark W. Täte, Marianne S. Hromalik, Lucas J. Koerner, Niels van Bakel, J. Morse, W. 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, Nicuşor Tı̂mneanu, Dingjie Wang, Nadia A. Zatsepin, Donald W. Schafer, James Defever, Richard Neutze, Petra Fromme, John C. H. Spence, Henry N. Chapman, Ilme Schlichting,

Advanced Electron Microscopy Techniques and Applications

Size Matters Less X-ray crystallography is a central research tool for uncovering the structures of proteins and other macromolecules. However, its applicability typically requires growth of large crystals, in part because a sufficient number of molecules must be present in the lattice for the sample to withstand x-ray—induced damage. Boutet et al. (p. 362 , published online 31 May) now demonstrate that the intense x-ray pulses emitted by a free-electron laser source can yield data in few enough exposures to uncover the high-resolution structure of microcrystals.