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@ARTICLE{Chapman:151178,
      author       = {Chapman, Henry N. and Fromme, Petra and Barty, Anton and
                      White, Thomas A. and Kirian, Richard A. and Aquila, Andrew
                      and Hunter, Mark S. and Schulz, Joachim and DePonte, Daniel
                      P. and Weierstall, Uwe and Doak, R. Bruce and Maia, Filipe
                      R. N. C. and Martin, Andrew V. and Schlichting, Ilme and
                      Lomb, Lukas and Coppola, Nicola and Shoeman, Robert L. and
                      Epp, Sascha W. and Hartmann, Robert and Rolles, Daniel and
                      Rudenko, Artem and Foucar, Lutz and Kimmel, Nils and
                      Weidenspointner, Georg and Holl, Peter and Liang, Mengning
                      and Barthelmess, Miriam and Caleman, Carl and Boutet,
                      Sébastien and Bogan, Michael J. and Krzywinski, Jacek and
                      Bostedt, Christoph and Bajt, Saša and Gumprecht, Lars and
                      Rudek, Benedikt and Erk, Benjamin and Schmidt, Carlo and
                      Hömke, André and Reich, Christian and Pietschner, Daniel
                      and Strüder, Lothar and Hauser, Günter and Gorke, Hubert
                      and Ullrich, Joachim and Herrmann, Sven and Schaller,
                      Gerhard and Schopper, Florian and Soltau, Heike and Kühnel,
                      Kai-Uwe and Messerschmidt, Marc and Bozek, John D. and
                      Hau-Riege, Stefan P. and Frank, Matthias and Hampton,
                      Christina Y. and Sierra, Raymond G. and Starodub, Dmitri and
                      Williams, Garth J. and Hajdu, Janos and Timneanu, Nicusor
                      and Seibert, M. Marvin and Andreasson, Jakob and Rocker,
                      Andrea and Jönsson, Olof and Svenda, Martin and Stern,
                      Stephan and Nass, Karol and Andritschke, Robert and
                      Schröter, Claus-Dieter and Krasniqi, Faton and Bott, Mario
                      and Schmidt, Kevin E. and Wang, Xiaoyu and Grotjohann, Ingo
                      and Holton, James M. and Barends, Thomas R. M. and Neutze,
                      Richard and Marchesini, Stefano and Fromme, Raimund and
                      Schorb, Sebastian and Rupp, Daniela and Adolph, Marcus and
                      Gorkhover, Tais and Andersson, Inger and Hirsemann, Helmut
                      and Potdevin, Guillaume and Graafsma, Heinz and Nilsson,
                      Björn and Spence, John C. H.},
      title        = {{F}emtosecond {X}-ray protein nanocrystallography},
      journal      = {Nature},
      volume       = {470},
      number       = {7332},
      issn         = {1476-4687},
      address      = {London [u.a.]},
      publisher    = {Nature Publising Group},
      reportid     = {FZJ-2014-01177},
      pages        = {73 - 77},
      year         = {2011},
      abstract     = {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.},
      cin          = {ZEA-2},
      ddc          = {070},
      cid          = {I:(DE-Juel1)ZEA-2-20090406},
      pnm          = {531 - Hadron Structure and Dynamics (HSD) (POF2-531)},
      pid          = {G:(DE-HGF)POF2-531},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000286886400036},
      pubmed       = {pmid:21293373},
      doi          = {10.1038/nature09750},
      url          = {https://juser.fz-juelich.de/record/151178},
}