Open AccessExploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models
Author(s) -
Keegan Ronan M.,
Bibby Jaclyn,
Thomas Jens,
Xu Dong,
Zhang Yang,
Mayans Olga,
Winn Martyn D.,
Rigden Daniel J.
Publication year - 2015
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s1399004714025784
Subject(s) - ab initio , quark , physics , particle physics , nuclear physics , computational chemistry , chemistry , quantum mechanics
AMPLE clusters and truncates ab initio protein structure predictions, producing search models for molecular replacement. Here, an interesting degree of complementarity is shown between targets solved using the different ab initio modelling programs QUARK and ROSETTA . Search models derived from either program collectively solve almost all of the all‐helical targets in the test set. Initial solutions produced by Phaser after only 5 min perform surprisingly well, improving the prospects for in situ structure solution by AMPLE during synchrotron visits. Taken together, the results show the potential for AMPLE to run more quickly and successfully solve more targets than previously suspected.