% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Zhou:311643,
      author       = {Zhou, X. Edward and Gao, Xiang and Barty, Anton and Kang,
                      Yanyong and He, Yuanzheng and liu, wei and Ishchenko, Andrii
                      and White, Thomas and Yefanov, Oleksandr and Han, Gye Won
                      and Xu, Qingping and de Waal, Parker W. and Suino-Powell,
                      Kelly M. and Boutet, Sébastien and Williams, Garth J. and
                      Wang, Meitian and Li, Dianfan and Caffrey, Martin and
                      Chapman, Henry N. and Spence, John C. H. and Fromme, Petra
                      and Weierstall, Uwe and Stevens, Raymond C. and Cherezov,
                      Vadim and Melcher, Karsten and Xu, H. Eric},
      title        = {{X}-ray laser diffraction for structure determination of
                      the rhodopsin-arrestin complex},
      journal      = {Scientific data},
      volume       = {3},
      issn         = {2052-4463},
      address      = {London},
      publisher    = {Nature Publ. Group},
      reportid     = {PUBDB-2016-04951},
      pages        = {160021},
      year         = {2016},
      note         = {URL of special issue:
                      http://www.nature.com/sdata/collections/xfel-biodata},
      abstract     = {Serial femtosecond X-ray crystallography (SFX) using an
                      X-ray free electron laser (XFEL) is a recent advancement in
                      structural biology for solving crystal structures of
                      challenging membrane proteins, including G-protein coupled
                      receptors (GPCRs), which often only produce microcrystals.
                      An XFEL delivers highly intense X-ray pulses of femtosecond
                      duration short enough to enable the collection of single
                      diffraction images before significant radiation damage to
                      crystals sets in. Here we report the deposition of the XFEL
                      data and provide further details on crystallization, XFEL
                      data collection and analysis, structure determination, and
                      the validation of the structural model. The
                      rhodopsin-arrestin crystal structure solved with SFX
                      represents the first near-atomic resolution structure of a
                      GPCR-arrestin complex, provides structural insights into
                      understanding of arrestin-mediated GPCR signaling, and
                      demonstrates the great potential of this SFX-XFEL technology
                      for accelerating crystal structure determination of
                      challenging proteins and protein complexes.},
      cin          = {FS-CFEL-1 / CFEL-I},
      ddc          = {610},
      cid          = {I:(DE-H253)FS-CFEL-1-20120731 / I:(DE-H253)CFEL-I-20161114},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      CUI - Hamburger Zentrum für ultraschnelle Beobachtung
                      (194651731)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(GEPRIS)194651731},
      experiment   = {EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000390214400001},
      pubmed       = {pmid:27070998},
      doi          = {10.1038/sdata.2016.21},
      url          = {https://bib-pubdb1.desy.de/record/311643},
}