The segmented anisotropic refinement of monoclinic papain by the application of the rigid-body TLS model and comparison to bovine ribonuclease A
- 1 February 1992
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta crystallographica Section B, Structural science, crystal engineering and materials
- Vol. 48 (1) , 67-75
- https://doi.org/10.1107/s0108768191006663
Abstract
The anisotropic displacements of selected rigid groups in monoclinic papain have been refined from X-ray diffraction data by application of the rigid-body TLS model. The rigid groups chosen were the aromatic side chains of tryptophan, tyrosine, histidine and phenylalanine, and the planar carboxylic and guanidinium side chains of aspartic acid, glutamic acid, glutamine, asparagine and arginine. The derived translation and libration tensors have been compared with those previously derived for bovine ribonuclease A and provide evidence for different modes and anisotropies of displacement over the two proteins.Keywords
This publication has 0 references indexed in Scilit: