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@ARTICLE{Lieske:422773,
      author       = {Lieske, Julia and Cerv, Maximilian and Kreida, Stefan and
                      Komadina, Dana and Fischer, Janine and Barthelmess, Miriam
                      and Fischer, Pontus and Pakendorf, Tim and Yefanov,
                      Oleksandr and Mariani, Valerio and Seine, Thomas and Ross,
                      Breyan H. and Crosas, Eva and Lorbeer, Olga and Burkhardt,
                      Anja and Lane, Thomas J. and Guenther, Sebastian and
                      Bergtholdt, Julian and Schoen, Silvan and
                      Törnroth-Horsefield, Susanna and Chapman, Henry N. and
                      Meents, Alke},
      title        = {{O}n-{C}hip {C}rystallization for {S}erial
                      {C}rystallopgraphy {E}xperiments and {O}n-{C}hip {L}igand
                      {B}inding {S}tudies},
      journal      = {IUCrJ},
      volume       = {2019},
      number       = {4},
      issn         = {2052-2525},
      address      = {Chester},
      reportid     = {PUBDB-2019-02326},
      pages        = {714-728},
      year         = {2019},
      note         = {© International Union of Crystallography},
      abstract     = {Efficient and reliable sample delivery has remained one of
                      the bottlenecks for serial crystallography experiments.
                      Compared with other methods, fixed-target sample delivery
                      offers the advantage of significantly reduced sample
                      consumption and shorter data collection times owing to
                      higher hit rates. Here, a new method of on-chip
                      crystallization is reported which allows the efficient and
                      reproducible growth of large numbers of protein crystals
                      directly on micro-patterned silicon chips for in-situ serial
                      crystallography experiments. Crystals are grown by
                      sitting-drop vapor diffusion and previously established
                      crystallization conditions can be directly applied. By
                      reducing the number of crystal-handling steps, the method is
                      particularly well suited for sensitive crystal systems.
                      Excessive mother liquor can be efficiently removed from the
                      crystals by blotting, and no sealing of the fixed-target
                      sample holders is required to prevent the crystals from
                      dehydrating. As a consequence, `naked' crystals are obtained
                      on the chip, resulting in very low background scattering
                      levels and making the crystals highly accessible for
                      external manipulation such as the application of ligand
                      solutions. Serial diffraction experiments carried out at
                      cryogenic temperatures at a synchrotron and at room
                      temperature at an X-ray free-electron laser yielded
                      high-quality X-ray structures of the human membrane protein
                      aquaporin 2 and two new ligand-bound structures of
                      thermolysin and the human kinase DRAK2. The results
                      highlight the applicability of the method for future
                      high-throughput on-chip screening of pharmaceutical
                      compounds.},
      cin          = {CFEL-I / FS-CFEL-1},
      ddc          = {530},
      cid          = {I:(DE-H253)CFEL-I-20161114 / I:(DE-H253)FS-CFEL-1-20120731},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G3 - PETRA III (POF3-622) / AXSIS - Frontiers in Attosecond
                      X-ray Science: Imaging and Spectroscopy (609920) / EUCALL -
                      European Cluster of Advanced Laser Light Sources (654220) /
                      SWEDEN-DESY - SWEDEN-DESY Collaboration
                      $(2020_Join2-SWEDEN-DESY)$},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G3 /
                      G:(EU-Grant)609920 / G:(EU-Grant)654220 /
                      $G:(DE-HGF)2020_Join2-SWEDEN-DESY$},
      experiment   = {EXP:(DE-H253)P-P11-20150101 /
                      EXP:(DE-H253)CFEL-Exp-20150101 /
                      EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31316815},
      UT           = {WOS:000473692700024},
      doi          = {10.1107/S2052252519007395},
      url          = {https://bib-pubdb1.desy.de/record/422773},
}