TY  - JOUR
AU  - Chapman, Henry N.
AU  - Fromme, Petra
AU  - Barty, Anton
AU  - White, Thomas A.
AU  - Kirian, Richard A.
AU  - Aquila, Andrew
AU  - Hunter, Mark S.
AU  - Schulz, Joachim
AU  - DePonte, Daniel P.
AU  - Weierstall, Uwe
AU  - Doak, R. Bruce
AU  - Maia, Filipe R. N. C.
AU  - Martin, Andrew V.
AU  - Schlichting, Ilme
AU  - Lomb, Lukas
AU  - Coppola, Nicola
AU  - Shoeman, Robert L.
AU  - Epp, Sascha W.
AU  - Hartmann, Robert
AU  - Rolles, Daniel
AU  - Rudenko, Artem
AU  - Foucar, Lutz
AU  - Kimmel, Nils
AU  - Weidenspointner, Georg
AU  - Holl, Peter
AU  - Liang, Mengning
AU  - Barthelmess, Miriam
AU  - Caleman, Carl
AU  - Boutet, Sébastien
AU  - Bogan, Michael J.
AU  - Krzywinski, Jacek
AU  - Bostedt, Christoph
AU  - Bajt, Saša
AU  - Gumprecht, Lars
AU  - Rudek, Benedikt
AU  - Erk, Benjamin
AU  - Schmidt, Carlo
AU  - Hömke, André
AU  - Reich, Christian
AU  - Pietschner, Daniel
AU  - Strüder, Lothar
AU  - Hauser, Günter
AU  - Gorke, Hubert
AU  - Ullrich, Joachim
AU  - Herrmann, Sven
AU  - Schaller, Gerhard
AU  - Schopper, Florian
AU  - Soltau, Heike
AU  - Kühnel, Kai-Uwe
AU  - Messerschmidt, Marc
AU  - Bozek, John D.
AU  - Hau-Riege, Stefan P.
AU  - Frank, Matthias
AU  - Hampton, Christina Y.
AU  - Sierra, Raymond G.
AU  - Starodub, Dmitri
AU  - Williams, Garth J.
AU  - Hajdu, Janos
AU  - Timneanu, Nicusor
AU  - Seibert, M. Marvin
AU  - Andreasson, Jakob
AU  - Rocker, Andrea
AU  - Jönsson, Olof
AU  - Svenda, Martin
AU  - Stern, Stephan
AU  - Nass, Karol
AU  - Andritschke, Robert
AU  - Schröter, Claus-Dieter
AU  - Krasniqi, Faton
AU  - Bott, Mario
AU  - Schmidt, Kevin E.
AU  - Wang, Xiaoyu
AU  - Grotjohann, Ingo
AU  - Holton, James M.
AU  - Barends, Thomas R. M.
AU  - Neutze, Richard
AU  - Marchesini, Stefano
AU  - Fromme, Raimund
AU  - Schorb, Sebastian
AU  - Rupp, Daniela
AU  - Adolph, Marcus
AU  - Gorkhover, Tais
AU  - Andersson, Inger
AU  - Hirsemann, Helmut
AU  - Potdevin, Guillaume
AU  - Graafsma, Heinz
AU  - Nilsson, Björn
AU  - Spence, John C. H.
TI  - Femtosecond X-ray protein nanocrystallography
JO  - Nature 
VL  - 470
IS  - 7332
SN  - 1476-4687
CY  - London [u.a.]
PB  - Nature Publising Group
M1  - FZJ-2014-01177
SP  - 73 - 77
PY  - 2011
AB  - X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded1, 2, 3. It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been determined despite their importance in all living cells. Here we present a method for structure determination where single-crystal X-ray diffraction ‘snapshots’ are collected from a fully hydrated stream of nanocrystals using femtosecond pulses from a hard-X-ray free-electron laser, the Linac Coherent Light Source4. We prove this concept with nanocrystals of photosystem I, one of the largest membrane protein complexes5. More than 3,000,000 diffraction patterns were collected in this study, and a three-dimensional data set was assembled from individual photosystem I nanocrystals (~200 nm to 2 μm in size). We mitigate the problem of radiation damage in crystallography by using pulses briefer than the timescale of most damage processes6. This offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000286886400036
C6  - pmid:21293373
DO  - DOI:10.1038/nature09750
UR  - https://juser.fz-juelich.de/record/151178
ER  -