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      REFMAC5 for the refinement of macromolecular crystal structures

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          Abstract

          The general principles behind the macromolecular crystal structure refinement program REFMAC5 are described.

          Abstract

          This paper describes various components of the macromolecular crystallographic refinement program REFMAC5, which is distributed as part of the CCP4 suite. REFMAC5 utilizes different likelihood functions depending on the diffraction data employed (amplitudes or intensities), the presence of twinning and the availability of SAD/SIRAS experimental diffraction data. To ensure chemical and structural integrity of the refined model, REFMAC5 offers several classes of restraints and choices of model parameterization. Reliable models at resolutions at least as low as 4 Å can be achieved thanks to low-resolution refinement tools such as secondary-structure restraints, restraints to known homologous structures, automatic global and local NCS restraints, ‘jelly-body’ restraints and the use of novel long-range restraints on atomic displacement parameters (ADPs) based on the Kullback–Leibler divergence. REFMAC5 additionally offers TLS parameterization and, when high-resolution data are available, fast refinement of anisotropic ADPs. Refinement in the presence of twinning is performed in a fully automated fashion. REFMAC5 is a flexible and highly optimized refinement package that is ideally suited for refinement across the entire resolution spectrum encountered in macromolecular crystallography.

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          Author and article information

          Conference
          Acta Crystallogr D Biol Crystallogr
          Acta Cryst. D
          Acta Crystallographica Section D: Biological Crystallography
          International Union of Crystallography
          0907-4449
          1399-0047
          01 April 2011
          18 March 2011
          18 March 2011
          : 67
          : Pt 4 ( publisher-idID: d110400 )
          : 355-367
          Affiliations
          [a ]Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, England
          [b ]Biophysical Structural Chemistry, Leiden University, PO Box 9502, 2300 RA Leiden, The Netherlands
          [c ]Randall Division of Cell and Molecular Biophysics, New Hunt’s House, King’s College London, London, England
          [d ]STFC Daresbury Laboratory, Warrington WA4 4AD, England
          Author notes
          Correspondence e-mail: garib@ 123456ysbl.york.ac.uk
          ba5152 ABCRE6 S0907444911001314
          10.1107/S0907444911001314
          3069751
          21460454
          © Murshudov et al. 2011

          This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

          Proceedings of the CCP4 study weekend
          Categories
          Research Papers

          Microscopy & Imaging

          refinement, refmac5

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