title: The use of protein homologues in the rotation function.
abstract: The success of molecular replacement depends, in part, on the degree of similarity of the target and search molecules. We have systematically investigated this effect in cross-rotation functions for members of the aspartic proteinase family of enzymes. The influence of various parameters on peak heights was investigated for six search models using magnitude of F(obs) data for two target enzymes. The beneficial effects of high-resolution data and a large radius of integration are most pronounced when target and search molecules have high-percentage identities. Correction for small differences in domain-domain orientation (typically 4-8 degrees) between search and target structures leads to only a marginal improvement in the rotation-function peak height. There is an almost linear relationship between the structural distance, D, a parameter used in cluster analysis to define differences between three-dimensional protein structures, and the height of the cross-rotation-function peaks.
authors.affiliation: Department of Crystallography, Birkbeck College, London, England.
authors.forename: C F
authors.initials: CF
authors.lastname: Aguilar
authors.forename: M P
authors.initials: MP
authors.lastname: Newman
authors.forename: J
authors.initials: J
authors.lastname: Sanz Aparicio
authors.forename: J B
authors.initials: JB
authors.lastname: Cooper
authors.forename: I J
authors.initials: IJ
authors.lastname: Tickle
authors.forename: T L
authors.initials: TL
authors.lastname: Blundell
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003198:Computer Simulation; D003460:Crystallization; D015394:Molecular Structure; D014961:X-Ray Diffraction
chemical_list: D016282:Aspartic Acid Endopeptidases; C042466:Endothia aspartic proteinase