Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements
|Authors:||Anton Barty, Carl Caleman, Andrew Aquila, Nicusor Timneanu, Lukas Lomb, Thomas A. White, Jakob Andreasson, David Arnlund, Saša Bajt, Thomas R. M. Barends, Miriam Barthelmess, Michael J. Bogan, Christoph Bostedt, John D. Bozek, Ryan Coffee, Nicola Coppola, Jan Davidsson, Daniel P. DePonte, R. Bruce Doak, Tomas Ekeberg, Veit Elser, Sascha W. Epp, Benjamin Erk, Holger Fleckenstein, Lutz Foucar, Petra Fromme, Heinz Graafsma, Lars Gumprecht, Janos Hajdu, Christina Y. Hampton, Robert Hartmann, Andreas Hartmann, Günter Hauser, Helmut Hirsemann, Peter Holl, Mark S. Hunter, Linda Johansson, Stephan Kassemeyer, Nils Kimmel, Richard A. Kirian, Mengning Liang, Filipe R. N. C. Maia, Erik Malmerberg, Stefano Marchesini, Andrew V. Martin, Karol Nass, Richard Neutze, Christian Reich, Daniel Rolles, Benedikt Rudek, Artem Rudenko, Howard Scott, Ilme Schlichting, Joachim Schulz, M. Marvin Seibert, Robert L. Shoeman, Raymond G. Sierra, Heike Soltau, John C. H. Spence, Francesco Stellato, Stephan Stern, Lothar Strüder, Joachim Ullrich, X. Wang, Georg Weidenspointner, Uwe Weierstall, Cornelia B. Wunderer, Henry N. Chapman|
|CellNetworks People:||Schlichting Ilme|
|Journal:||Nature Photonics 6, 35–40 (2012) doi:10.1038/nphoton.2011.297|
X-ray free-electron lasers have enabled new approaches to the structural determination of protein crystals that are too small or radiation-sensitive for conventional analysis1. For sufficiently short pulses, diffraction is collected before significant changes occur to the sample, and it has been predicted that pulses as short as 10 fs may be required to acquire atomic-resolution structural information1, 2, 3, 4. Here, we describe a mechanism unique to ultrafast, ultra-intense X-ray experiments that allows structural information to be collected from crystalline samples using high radiation doses without the requirement for the pulse to terminate before the onset of sample damage. Instead, the diffracted X-rays are gated by a rapid loss of crystalline periodicity, producing apparent pulse lengths significantly shorter than the duration of the incident pulse. The shortest apparent pulse lengths occur at the highest resolution, and our measurements indicate that current X-ray free-electron laser technology5 should enable structural determination from submicrometre protein crystals with atomic resolution.