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@ARTICLE{Chapman:169302,
      author       = {Chapman, H. N. and Caleman, C. and Timneanu, N.},
      title        = {{D}iffraction before destruction},
      journal      = {Philosophical transactions of the Royal Society of London /
                      B},
      volume       = {369},
      number       = {1647},
      issn         = {1471-2970},
      address      = {London},
      publisher    = {JSTOR},
      reportid     = {DESY-2014-02888},
      pages        = {20130313},
      year         = {2014},
      abstract     = {X-ray free-electron lasers have opened up the possibility
                      of structure determination of protein crystals at room
                      temperature, free of radiation damage. The
                      femtosecond-duration pulses of these sources enable
                      diffraction signals to becollected from samples at doses of
                      1000 MGy or higher. The sample is vaporized by the intense
                      pulse, but not before the scattering that gives rise to the
                      diffraction pattern takes place. Consequently, only a single
                      flash diffraction pattern can be recorded from a crystal,
                      giving rise to the method of serial crystallography where
                      tens of thousands of patterns are ollected from individual
                      crystals that flow across the beam and the patterns are
                      indexed and aggregated into a set of structure factors. The
                      high-dose tolerance and the many-crystal averaging approach
                      allow data to be collected from much smaller crystals than
                      have been examined at synchrotron radiation facilities, even
                      from radiation-sensitive samples. Here, we review the
                      interaction of intense femtosecond X-ray pulses with
                      materials and discuss the implications forstructure
                      determination. We identify various dose regimes and conclude
                      that the strongest achievable signals for a given sample are
                      attained at the highest possible dose rates, from highest
                      possible pulse intensities.},
      cin          = {FS-CFEL-1},
      ddc          = {570},
      cid          = {I:(DE-H253)FS-CFEL-1-20120731},
      pnm          = {Experiments at CFEL (POF2-544)},
      pid          = {G:(DE-H253)POF2-CFEL-Exp.-20130405},
      experiment   = {EXP:(DE-H253)CFEL-Exp-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000337367600003},
      pubmed       = {pmid:24914146},
      doi          = {10.1098/rstb.2013.0313},
      url          = {https://bib-pubdb1.desy.de/record/169302},
}