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@ARTICLE{Nogly:207438,
      author       = {Nogly, Przemyslaw and James, Daniel and Wang, Dingjie and
                      White, Thomas A. and Zatsepin, Nadia and Shilova, Anastasya
                      and Nelson, Garrett and Liu, Haiguang and Johansson, Linda
                      and Heymann, Michael and Jaeger, Kathrin and Metz, Markus
                      and Wickstrand, Cecilia and Wu, Wenting and Båth, Petra and
                      Berntsen, Peter and Oberthuer, Dominik and Panneels, Valerie
                      and Cherezov, Vadim and Chapman, Henry and Schertler,
                      Gebhard and Neutze, Richard and Spence, John and Moraes,
                      Isabel and Burghammer, Manfred and Standfuss, Joerg and
                      Weierstall, Uwe},
      title        = {{L}ipidic {C}ubic {P}hase {S}erial {M}illisecond
                      {C}rystallography using {S}ynchrotron {R}adiation},
      journal      = {IUCrJ},
      volume       = {2},
      number       = {2},
      issn         = {2052-2525},
      address      = {Chester},
      publisher    = {International Union of Crystallography (IUCr)},
      reportid     = {PUBDB-2015-01346},
      pages        = {168 - 176},
      year         = {2015},
      note         = {PIF-2015-46},
      abstract     = {Lipidic cubic phases (LCPs) have emerged as successful
                      matrixes for the crystallization of membrane
                      proteins.Moreover, the viscous LCP also provides a highly
                      effective delivery medium for serial femtosecond
                      crystallography (SFX) at X-ray free-electron lasers (XFELs).
                      Here, the adaptation of this technology to perform serial
                      millisecond crystallography (SMX) at more widely available
                      synchrotron microfocus beamlines is described. Compared with
                      conventional microcrystallography, LCP-SMX eliminates the
                      need for difficult handling of individual crystals and
                      allows for data collection at room temperature. The
                      technology is demonstrated by solving a structure of the
                      light-driven protonpump bacteriorhodopsin (bR) at a
                      resolution of 2.4 A ° . The room-temperature structure of
                      bR is very similar to previous cryogenic structures but
                      shows small yet distinct differences in the retinal ligand
                      and proton-transfer pathway.},
      cin          = {FS-CFEL-1},
      ddc          = {530},
      cid          = {I:(DE-H253)FS-CFEL-1-20120731},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      NANOMEM - Membrane Protein Nanocrystallography (317079)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(EU-Grant)317079},
      experiment   = {EXP:(DE-H253)CFEL-Exp-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000356866400007},
      pubmed       = {pmid:25866654},
      doi          = {10.1107/S2052252514026487},
      url          = {https://bib-pubdb1.desy.de/record/207438},
}