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@ARTICLE{Hunter:207279,
      author       = {Hunter, Mark S. and Segelke, Brent and Messerschmidt, Marc
                      and Williams, Garth J. and Zatsepin, Nadia A. and Barty,
                      Anton and Benner, W. Henry and Carlson, David B. and
                      Coleman, Matthew and Graf, Alexander and Hau-Riege, Stefan
                      P. and Pardini, Tommaso and Seibert, M. Marvin and Evans,
                      James and Boutet, Sébastien and Frank, Matthias},
      title        = {{F}ixed-{T}arget {P}rotein {S}erial {M}icrocrystallography
                      with an {X}-ray {F}ree {E}lectron {L}aser},
      journal      = {Scientific reports},
      volume       = {4},
      number       = {6026},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {PUBDB-2015-01262},
      pages        = {1},
      year         = {2014},
      note         = {OA},
      abstract     = {We present results from experiments at the Linac Coherent
                      Light Source (LCLS) demonstrating that serial femtosecond
                      crystallography (SFX) can be performed to high resolution
                      (~2.5 Å) using protein microcrystals deposited on an
                      ultra-thin silicon nitride membrane and embedded in a
                      preservation medium at room temperature. Data can be
                      acquired at a high acquisition rate using x-ray free
                      electron laser sources to overcome radiation damage, while
                      sample consumption is dramatically reduced compared to
                      flowing jet methods. We achieved a peak data acquisition
                      rate of 10 Hz with a hit rate of $~38\%,$ indicating that
                      a complete data set could be acquired in about one 12-hour
                      LCLS shift using the setup described here, or in even less
                      time using hardware optimized for fixed target SFX. This
                      demonstration opens the door to ultra low sample consumption
                      SFX using the technique of diffraction-before-destruction on
                      proteins that exist in only small quantities and/or do not
                      produce the copious quantities of microcrystals required for
                      flowing jet methods.},
      cin          = {FS-CFEL-1},
      ddc          = {000},
      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:000340674000004},
      pubmed       = {pmid:25113598},
      doi          = {10.1038/srep06026},
      url          = {https://bib-pubdb1.desy.de/record/207279},
}