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@ARTICLE{Brunger:111909,
      author       = {Brunger, A.T. and Adams, P.D. and Fromme, P. and Fromme, R.
                      and Levitt, M. and Schröder, G.F.},
      title        = {{I}mproving the accuracy of macromolecular structure
                      refinement at 7 Å resolution},
      journal      = {Structure},
      volume       = {20},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PreJuSER-111909},
      pages        = {957 - 966},
      year         = {2012},
      note         = {Record converted from VDB: 16.11.2012},
      abstract     = {In X-ray crystallography, molecular replacement
                      and subsequent refinement is challenging at low resolution.
                      We compared refinement methods using synchrotron diffraction
                      data of photosystem I at 7.4 Å resolution, starting from
                      different initial models with increasing deviations from the
                      known high-resolution structure. Standard refinement spoiled
                      the initial models, moving them further away from the true
                      structure and leading to high R(free)-values. In contrast,
                      DEN refinement improved even the most distant starting model
                      as judged by R(free), atomic root-mean-square differences to
                      the true structure, significance of features not included in
                      the initial model, and connectivity of electron density. The
                      best protocol was DEN refinement with initial segmented
                      rigid-body refinement. For the most distant initial model,
                      the fraction of atoms within 2 Å of the true structure
                      improved from $24\%$ to $60\%.$ We also found a significant
                      correlation between R(free) values and the accuracy of the
                      model, suggesting that R(free) is useful even at low
                      resolution.},
      keywords     = {Bacterial Proteins: chemistry / Crystallography, X-Ray /
                      Models, Molecular / Photosystem I Protein Complex: chemistry
                      / Protein Structure, Secondary / Protein Structure, Tertiary
                      / Software / Structural Homology, Protein / Bacterial
                      Proteins (NLM Chemicals) / Photosystem I Protein Complex
                      (NLM Chemicals)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22681901},
      pmc          = {pmc:PMC3380535},
      UT           = {WOS:000305094500004},
      doi          = {10.1016/j.str.2012.04.020},
      url          = {https://juser.fz-juelich.de/record/111909},
}