Time-resolved protein nanocrystallography using an X-ray free-electron laser

Andrew Aquila, Mark S. Hunter, R. Bruce Doak, Richard A. Kirian, Petra Fromme, Thomas A. White, Jakob Andreasson, David Arnlund, Saša Bajt, Thomas R.M. Barends, Miriam Barthelmess, Michael J. Bogan, Christoph Bostedt, Hervé Bottin, John D. Bozek, Carl Caleman, Nicola Coppola, Jan Davidsson, Daniel P. Deponte, Veit ElserSascha W. Epp, Benjamin Erk, Holger Fleckenstein, Lutz Foucar, Matthias Frank, Raimund Fromme, Heinz Graafsma, Ingo Grotjohann, Lars Gumprecht, Janos Hajdu, Christina Y. Hampton, Andreas Hartmann, Robert Hartmann, Stefan Hau-Riege, Günter Hauser, Helmut Hirsemann, Peter Holl, James M. Holton, André Hömke, Linda Johansson, Nils Kimmel, Stephan Kassemeyer, Faton Krasniqi, Kai Uwe Kühnel, Mengning Liang, Lukas Lomb, Erik Malmerberg, Stefano Marchesini, Andrew V. Martin, Filipe R.N.C. Maia, Marc Messerschmidt, Karol Nass, Christian Reich, Richard Neutze, Daniel Rolles, Benedikt Rudek, Artem Rudenko, Ilme Schlichting, Carlo Schmidt, Kevin E. Schmidt, Joachim Schulz, M. Marvin Seibert, Robert L. Shoeman, Raymond Sierra, Heike Soltau, Dmitri Starodub, Francesco Stellato, Stephan Stern, Lothar Strüder, Nicusor Timneanu, Joachim Ullrich, Xiaoyu Wang, Garth J. Williams, Georg Weidenspointner, Uwe Weierstall, Cornelia Wunderer, Anton Barty, John C.H. Spence, Henry N. Chapman

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Abstract

We demonstrate the use of an X-ray free electron laser synchronized with an optical pump laser to obtain X-ray diffraction snapshots from the photoactivated states of large membrane protein complexes in the form of nanocrystals flowing in a liquid jet. Light-induced changes of Photosystem I-Ferredoxin co-crystals were observed at time delays of 5 to 10 μs after excitation. The result correlates with the microsecond kinetics of electron transfer from Photosystem I to ferredoxin. The undocking process that follows the electron transfer leads to large rearrangements in the crystals that will terminally lead to the disintegration of the crystals. We describe the experimental setup and obtain the first timeresolved femtosecond serial X-ray crystallography results from an irreversible photo-chemical reaction at the Linac Coherent Light Source. This technique opens the door to time-resolved structural studies of reaction dynamics in biological systems.

Original languageEnglish
Pages (from-to)2706-2716
Number of pages11
JournalOptics express
Volume20
Issue number3
DOIs
Publication statusPublished - Jan 30 2012

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ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics

Cite this

Aquila, A., Hunter, M. S., Doak, R. B., Kirian, R. A., Fromme, P., White, T. A., Andreasson, J., Arnlund, D., Bajt, S., Barends, T. R. M., Barthelmess, M., Bogan, M. J., Bostedt, C., Bottin, H., Bozek, J. D., Caleman, C., Coppola, N., Davidsson, J., Deponte, D. P., ... Chapman, H. N. (2012). Time-resolved protein nanocrystallography using an X-ray free-electron laser. Optics express, 20(3), 2706-2716. https://doi.org/10.1364/OE.20.002706