High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

• DOI: 10.1126/science.1217737
• Publication Date: 2012-06-01T04:14:27Z
• Authors: 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 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
• Keywords: Protein crystallization; Micrometer; Phaser

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 large crystals, in part because sufficient number molecules must be present lattice sample to withstand x-ray—induced damage. Boutet et al. (p. 362 , published online 31 May) now demonstrate that intense x-ray pulses emitted by free-electron laser source can yield data few enough exposures uncover high-resolution structure microcrystals.