|
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. 690
Section 25.1.6.2. DM/DMMULTI
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 |
DM
(Cowtan, 1994![[link]](/graphics/greenarr.gif)
) is a density-modification program package. DM applies real-space constraints based on known features of a protein electron-density map in order to improve the approximate phasing obtained from experimental sources. Various information can be applied, including the following diverse elements: solvent flattening, histogram mapping, multi-resolution modification, NCS averaging, skeletonization and Sayre's equation. DM is part of the CCP4 suite (Section 25.1.2.4). See Chapter 15.1
and Section 25.2.2
for more details.
Operating systems: UNIX, VAX/VMS and LINUX. Type: source code and binary. Distribution: free academic.
References
Cowtan, K. (1994). DM: an automated procedure for phase improvement by density modification. CCP4 ESF-EACBM Newsl. Protein Crystallogr. 31, 34–38.Google Scholar
