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@ARTICLE{Efremov:40230,
      author       = {Efremov, R. and Moukhametzianov, R. and Büldt, G. and
                      Gordeliy, V. I.},
      title        = {{P}hysical {D}etwinning of {H}emihedrally {T}winned
                      {H}exagonal {C}rystals of {B}acteriorhdopsin},
      journal      = {Biophysical journal},
      volume       = {87},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-40230},
      pages        = {3608 - 3613},
      year         = {2004},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Hexagonal crystals of the membrane protein
                      bacteriorhodopsin of space group P6 3 grown in lipidic cubic
                      phase are twinned hemihedrally. It was shown that slow
                      changes of salt concentration in the mother liquor lead to a
                      split of crystals so that the split parts preserved high
                      diffraction quality. Analysis of diffraction data from split
                      crystals by Yeates statistic and Britton plot showed that
                      the split parts are free of twinning. It is concluded that
                      crystals of bacteriorhodopsin are composed of several
                      macroscopic twinning domains with sizes comparable to the
                      original crystal. The appearance of twinning domains during
                      crystal growth and the mechanism of splitting are
                      discussed.},
      keywords     = {Bacteriorhodopsins: analysis / Bacteriorhodopsins:
                      chemistry / Bacteriorhodopsins: ultrastructure / Binding
                      Sites / Computer Simulation / Crystallization: methods /
                      Crystallography: methods / Models, Chemical / Models,
                      Molecular / Multiprotein Complexes: chemistry / Multiprotein
                      Complexes: ultrastructure / Protein Binding / Multiprotein
                      Complexes (NLM Chemicals) / Bacteriorhodopsins (NLM
                      Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15339801},
      pmc          = {pmc:PMC1304826},
      UT           = {WOS:000224732500061},
      doi          = {10.1529/biophysj.104.046573},
      url          = {https://juser.fz-juelich.de/record/40230},
}