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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 25.1.5.5. RSRef
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 |
RSRef
(Chapman, 1995![[link]](/graphics/greenarr.gif)
) is a package of programs that enables an atomic model to be optimized by fitting to an electron-density map. RSRef uses an electron-density function that is resolution dependent, so that it accurately models a medium-resolution map. When combined with TNT's (Section 25.1.5.8) Geometry, full stereochemical refinement is possible. RSRef can be used to quickly pre-refine a protein structure during or after model building, or to completely refine structures with high noncrystallographic symmetry that have good electron density.
Location: http://www.sb.fsu.edu/∼rsref/ . Operating systems: SGI and EVS. Type: source code and binary. Distribution: minor licence fee for academic users.
References
Chapman, M. S. (1995). Restrained real-space macromolecular atomic refinement using a new resolution-dependent electron-density function. Acta Cryst. A51, 69–80.Google Scholar
