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@ARTICLE{Grinkevich:315131,
      author       = {Grinkevich, Pavel and Iermak, Iuliia and Luedtke, Nicholas
                      A. and Mesters, Jeroen R. and Ettrich, Rüdiger and Ludwig,
                      Jost},
      title        = {p{H}luorin-assisted expression, purification,
                      crystallization and {X}-ray diffraction data analysis of the
                      {C}-terminal domain of the {H}sd{R} subunit of the
                      {E}scherichia coli type {I} restriction-modification system
                      {E}co{R}124{I}},
      journal      = {Acta crystallographica / F},
      volume       = {72},
      number       = {9},
      issn         = {2053-230X},
      publisher    = {IUCr},
      reportid     = {PUBDB-2016-05653},
      pages        = {672 - 676},
      year         = {2016},
      note         = {(c) International Union of Crystallography},
      abstract     = {The HsdR subunit of the type I restriction-modification
                      system EcoR124I is responsible for the translocation as well
                      as the restriction activity of the whole complex consisting
                      of the HsdR, HsdM and HsdS subunits, and while crystal
                      structures are available for the wild type and several
                      mutants, the C-terminal domain comprising approximately 150
                      residues was not resolved in any of these structures. Here,
                      three fusion constructs with the GFP variant pHluorin
                      developed to overexpress, purify and crystallize the
                      C-terminal domain of HsdR are reported. The shortest of the
                      three encompassed HsdR residues 887-1038 and yielded
                      crystals that belonged to the orthorhombic space group
                      C222$_1$, with unit-cell parameters a = 83.42, b = 176.58, c
                      = 126.03 Å, $\alpha$ = $\beta$ = $\gamma$ = 90.00° and two
                      molecules in the asymmetric unit (V$_M$ = 2.55 Å$^3$
                      Da$^{-1}$, solvent content 50.47\%). X-ray diffraction data
                      were collected to a resolution of 2.45 Å.},
      cin          = {EMBL-User},
      ddc          = {530},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (POF3-622) / BIOSTRUCT-X - Transnational
                      access and enhancement of integrated Biological Structure
                      determination at synchrotron X-ray radiation facilities
                      (283570)},
      pid          = {G:(DE-HGF)POF3-6G3 / G:(EU-Grant)283570},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000384167800003},
      pubmed       = {pmid:27599856},
      doi          = {10.1107/S2053230X16011626},
      url          = {https://bib-pubdb1.desy.de/record/315131},
}