|
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 25.1.5.8. TNT
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 |
TNT
(Tronrud et al., 1987![[link]](/graphics/greenarr.gif)
; Tronrud, 1997) is a general-purpose program package for the structure refinement of macromolecules using single-crystal X-ray diffraction data. It is normally used to optimize a model to X-ray diffraction data while maintaining proper stereochemistry using least-squares function-minimization techniques. It can restrain a model to bond lengths, bond angles, dihedral angles, pseudo-rotation angles, planarity and non-bonded `close' contacts (including symmetry-related contacts). A principal advantage of the TNT package is its great flexibility, making it ideal for restraining structures that contain cofactors, inhibitors, or nucleic acids. The package is composed of separate programs, each performing clearly defined tasks. To use the package with other forms of data you simply write programs that produce the value and first derivative of the functional term you wish to minimize. See Section 25.2.4
for a detailed description.
Location: http://www.uoxray.uoregon.edu/tnt/welcome.html . Operating systems: UNIX, VAX/VMS, DEC Alpha, EVS, AIX, SUN and SGI. Type: source code and binary. Distribution: free academic.
References
Tronrud, D. E. (1997). The TNT refinement package. Methods Enzymol. 277, 306–319.Google Scholar
Tronrud, D. E., Ten Eyck, L. F. & Matthews, B. W. (1987). An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Cryst. A43, 489–501.Google Scholar
