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@ARTICLE{Meents:393805,
      author       = {Meents, Alke and Wiedorn, Max O. and Srajer, V. and
                      Henning, R. and Sarrou, Iosifina and Bergtholdt, Julian and
                      Barthelmess, Miriam and Reinke, P. Y. A. and Dierksmeyer,
                      Dennis and Tolstikova, A. and Schaible, S. and
                      Messerschmidt, M. and Ogata, C. M. and Kissick, D. J. and
                      Taft, M. H. and Manstein, D. J. and Lieske, Julia and
                      Oberthür, Dominik and Fischetti, R. F. and Chapman, Henry
                      N.},
      title        = {{P}ink-beam serial crystallography},
      journal      = {Nature Communications},
      volume       = {8},
      number       = {1},
      issn         = {2041-1723},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {PUBDB-2017-11676},
      pages        = {1281},
      year         = {2017},
      abstract     = {Serial X-ray crystallography allows macromolecular
                      structure determination at both X-ray free electron lasers
                      (XFELs) and, more recently, synchrotron sources. The time
                      resolution for serial synchrotron crystallography
                      experiments has been limited to millisecond timescales with
                      monochromatic beams. The polychromatic, “pink”, beam
                      provides a more than two orders of magnitude increased
                      photon flux and hence allows accessing much shorter
                      timescales in diffraction experiments at synchrotron
                      sources. Here we report the structure determination of two
                      different protein samples by merging pink-beam diffraction
                      patterns from many crystals, each collected with a single
                      100 ps X-ray pulse exposure per crystal using a setup
                      optimized for very low scattering background. In contrast to
                      experiments with monochromatic radiation, data from only 50
                      crystals were required to obtain complete datasets. The high
                      quality of the diffraction data highlights the potential of
                      this method for studying irreversible reactions at
                      sub-microsecond timescales using high-brightness X-ray
                      facilities.},
      cin          = {CFEL-I / FS-PS},
      ddc          = {500},
      cid          = {I:(DE-H253)CFEL-I-20161114 / I:(DE-H253)FS-PS-20131107},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      X-probe - Advanced XFEL and Synchrotron based Probes of
                      Protein Structure and Dynamics (637295) / BMBF-05K14CHA -
                      05K14CHA - SyncFELmed: Teilprojekt 2 (BMBF-05K14CHA) /
                      VH-VI-419 - Dynamic Pathways in Multidimensional Landscapes
                      (VH-VI-419) / VH-VI-403 - In-Situ Nano-Imaging of Biological
                      and Chemical Processes $(2015_IFV-VH-VI-403)$ / EUCALL -
                      European Cluster of Advanced Laser Light Sources (654220)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(EU-Grant)637295 /
                      G:(DE-H253)BMBF-05K14CHA / G:(DE-HGF)VH-VI-419 /
                      $G:(DE-HGF)2015_IFV-VH-VI-403$ / G:(EU-Grant)654220},
      experiment   = {EXP:(DE-H253)CFEL-Exp-20150101 /
                      EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29097720},
      UT           = {WOS:000414376600002},
      doi          = {10.1038/s41467-017-01417-3},
      url          = {https://bib-pubdb1.desy.de/record/393805},
}