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@ARTICLE{Panneels:275873,
      author       = {Panneels, Valérie and Wu, Wenting and Tsai, Ching-Ju and
                      Nogly, Przemek and Rheinberger, Jan and Jaeger, Kathrin and
                      Cicchetti, Gregor and Gati, Cornelius and Kick, Leonhard M.
                      and Sala, Leonardo and Capitani, Guido and Milne, Chris and
                      Padeste, Celestino and Pedrini, Bill and Li, Xiao-Dan and
                      Standfuss, Jörg and Abela, Rafael and Schertler, Gebhard},
      title        = {{T}ime-resolved structural studies with serial
                      crystallography: {A} new light on retinal proteins},
      journal      = {Structural dynamics},
      volume       = {2},
      number       = {4},
      issn         = {2329-7778},
      address      = {Melville, NY},
      publisher    = {AIP Publishing LLC},
      reportid     = {PUBDB-2015-04290},
      pages        = {041718},
      year         = {2015},
      abstract     = {Structural information of the different conformational
                      states of the two prototypical light-sensitive membrane
                      proteins, bacteriorhodopsin and rhodopsin, has been obtained
                      in the past by X-ray cryo-crystallography and cryo-electron
                      microscopy. However, these methods do not allow for the
                      structure determination of most intermediate conformations.
                      Recently, the potential of X-Ray Free Electron Lasers
                      (X-FELs) for tracking the dynamics of light-triggered
                      processes by pump-probe serial femtosecond crystallography
                      has been demonstrated using 3D-micron-sized crystals. In
                      addition, X-FELs provide new opportunities for protein
                      2D-crystal diffraction, which would allow to observe the
                      course of conformational changes of membrane proteins in a
                      close-to-physiological lipid bilayer environment. Here, we
                      describe the strategies towards structural dynamic studies
                      of retinal proteins at room temperature, using injector or
                      fixed-target based serial femtosecond crystallography at
                      X-FELs. Thanks to recent progress especially in sample
                      delivery methods, serial crystallography is now also
                      feasible at synchrotron X-ray sources, thus expanding the
                      possibilities for time-resolved structure determination.},
      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) /
                      X-probe - Advanced XFEL and Synchrotron based Probes of
                      Protein Structure and Dynamics (637295) / VH-GS-500 - PIER
                      Helmholtz Graduate School $(2015_IFV-VH-GS-500)$},
      pid          = {G:(DE-HGF)POF3-6215 / G:(EU-Grant)317079 /
                      G:(EU-Grant)637295 / $G:(DE-HGF)2015_IFV-VH-GS-500$},
      experiment   = {EXP:(DE-H253)CFEL-Exp-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000360649200020},
      pubmed       = {pmid:26798817},
      doi          = {10.1063/1.4922774},
      url          = {https://bib-pubdb1.desy.de/record/275873},
}