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@ARTICLE{Wu:275872,
      author       = {Wu, Wenting and Nogly, Przemyslaw and Rheinberger, Jan and
                      Kick, Leonhard M. and Gati, Cornelius and Nelson, Garrett
                      and Deupi, Xavier and Standfuss, Jörg and Schertler,
                      Gebhard and Panneels, Valérie},
      title        = {{B}atch crystallization of rhodopsin for structural
                      dynamics using an {X}-ray free-electron laser},
      journal      = {Acta crystallographica / F},
      volume       = {71},
      number       = {7},
      issn         = {2053-230X},
      address      = {Oxford [u.a.]},
      publisher    = {Blackwell},
      reportid     = {PUBDB-2015-04289},
      pages        = {856 - 860},
      year         = {2015},
      abstract     = {Rhodopsin is a membrane protein from the G protein-coupled
                      receptor family. Together with its ligand retinal, it forms
                      the visual pigment responsible for night vision. In order to
                      perform ultrafast dynamics studies, a time-resolved serial
                      femtosecond crystallography method is required owing to the
                      nonreversible activation of rhodopsin. In such an approach,
                      microcrystals in suspension are delivered into the X-ray
                      pulses of an X-ray free-electron laser (XFEL) after a
                      precise photoactivation delay. Here, a millilitre batch
                      production of high-density microcrystals was developed by
                      four methodical conversion steps starting from known
                      vapour-diffusion crystallization protocols: (i) screening
                      the low-salt crystallization conditions preferred for serial
                      crystallography by vapour diffusion, (ii) optimization of
                      batch crystallization, (iii) testing the crystal size and
                      quality using second-harmonic generation (SHG) imaging and
                      X-ray powder diffraction and (iv) production of millilitres
                      of rhodopsin crystal suspension in batches for serial
                      crystallography tests; these crystals diffracted at an XFEL
                      at the Linac Coherent Light Source using a liquid-jet
                      setup.},
      ddc          = {530},
      pnm          = {6211 - Extreme States of Matter: From Cold Ions to Hot
                      Plasmas (POF3-621) / NANOMEM - Membrane Protein
                      Nanocrystallography (317079)},
      pid          = {G:(DE-HGF)POF3-6211 / G:(EU-Grant)317079},
      experiment   = {EXP:(DE-H253)CFEL-Exp-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000357830700008},
      doi          = {10.1107/S2053230X15009966},
      url          = {https://bib-pubdb1.desy.de/record/275872},
}