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@ARTICLE{Kubicek:111979,
      author       = {Kubicek, J. and Schlesinger, R. and Baeken, C. and Büldt,
                      G. and Schäfer, F. and Labahn, J.},
      title        = {{C}ontrolled {I}n {M}eso {P}hase {C}rystallization -- {A}
                      {M}ethod for the {S}tructural {I}nvestigation of {M}embrane
                      {P}roteins},
      journal      = {PLoS one},
      volume       = {7},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PreJuSER-111979},
      pages        = {e35458},
      year         = {2012},
      note         = {Record converted from VDB: 16.11.2012},
      abstract     = {We investigated in meso crystallization of membrane
                      proteins to develop a fast screening technology which
                      combines features of the well established classical vapor
                      diffusion experiment with the batch meso phase
                      crystallization, but without premixing of protein and
                      monoolein. It inherits the advantages of both methods,
                      namely (i) the stabilization of membrane proteins in the
                      meso phase, (ii) the control of hydration level and additive
                      concentration by vapor diffusion. The new technology (iii)
                      significantly simplifies in meso crystallization experiments
                      and allows the use of standard liquid handling robots
                      suitable for 96 well formats. CIMP crystallization
                      furthermore allows (iv) direct monitoring of phase
                      transformation and crystallization events. Bacteriorhodopsin
                      (BR) crystals of high quality and diffraction up to 1.3 Å
                      resolution have been obtained in this approach. CIMP and the
                      developed consumables and protocols have been successfully
                      applied to obtain crystals of sensory rhodopsin II (SRII)
                      from Halobacterium salinarum for the first time.},
      keywords     = {Bacteriorhodopsins: chemistry / Crystallization /
                      Crystallography, X-Ray: methods / Glycerides: chemistry /
                      Halobacterium salinarum / Halorhodopsins: chemistry /
                      Membrane Proteins: chemistry / Phase Transition / Protein
                      Stability / Sensory Rhodopsins: chemistry / Glycerides (NLM
                      Chemicals) / Halorhodopsins (NLM Chemicals) / Membrane
                      Proteins (NLM Chemicals) / Sensory Rhodopsins (NLM
                      Chemicals) / sensory rhodopsin II protein, archaeal (NLM
                      Chemicals) / monoolein (NLM Chemicals) / Bacteriorhodopsins
                      (NLM Chemicals)},
      cin          = {ICS-5 / ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-5-20110106 / I:(DE-Juel1)ICS-6-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung / Funktion und Dysfunktion des
                      Nervensystems},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK409},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22536388},
      pmc          = {pmc:PMC3334905},
      UT           = {WOS:000305336200043},
      doi          = {10.1371/journal.pone.0035458},
      url          = {https://juser.fz-juelich.de/record/111979},
}