REFMAC 5 for the refinement of macromolecular crystal structures

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…

• WT
  Wellcome Trust

  Award: 064405
• NO
  Nederlandse Organisatie voor Wetenschappelijk Onderzoek
• BA
  Biotechnology and Biological Sciences Research Council

  Awards: BB/F020228/1, BB/F001134/1, BB/F020805/1