International
Tables for Crystallography Volume F Crystallography of biological macromolecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 25.1, p. 689
Section 25.1.5.4. REFMAC
a
Biomolecular Crystallography Laboratory, CABM & Rutgers University, 679 Hoes Lane, Piscataway, NJ 08854-5638, USA, and Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Yue-Yang Road, Shanghai 200 031, People's Republic of China, and bBiomolecular Crystallography Laboratory, CABM & Rutgers University, 679 Hoes Lane, Piscataway, NJ 08854-5638, USA |
REFMAC (Murshudov et al., 1997, 1999) is a macromolecular refinement program which has been integrated into the CCP4 suite (Section 25.1.2.4). REFMAC can carry out rigid-body, restrained or unrestrained refinement against X-ray data, or idealization of a macromolecular structure. It minimizes the coordinate parameters to satisfy either a maximum-likelihood or least-squares residual. There are options to use different minimization methods. If the user wishes to invoke geometric restraints, the program PROTIN, which analyses the protein geometry and produces an output file containing restraints information, must be run prior to running REFMAC. REFMAC also produces an MTZ output file containing weighted coefficients for SIGMAA-weighted mFo-DFcalc and 2mFo-DFcalc maps, where `missing data' have been restored.
Location: http://www.dl.ac.uk/CCP/CCP4/dist/html/refmac5.html . Operating systems: UNIX, SGI, SUN, DEC and LINUX. Type: source code and binary. Distribution: free.
References
Murshudov, G. N., Vagin, A. A. & Dodson, E. J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D53, 240–255.Google ScholarMurshudov, G. N., Vagin, A. A., Lebedev, A., Wilson, K. S. & Dodson, E. J. (1999). Efficient anisotropic refinement of macromolecular structures using FFT. Acta Cryst. D55, 247–255.Google Scholar