Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models

Keegan, Ronan M, Bibby, Jaclyn, Thomas, Jens ORCID: 0000-0003-0277-8505, Xu, Dong, Zhang, Yang, Mayans, Olga, Winn, Martyn D and Rigden, Daniel J ORCID: 0000-0002-7565-8937 (2015) Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 71 (Pt 2). pp. 338-343.

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Official URL: http://dx.doi.org/10.1107/s1399004714025784

Abstract

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.

Item Type:	Article
Uncontrolled Keywords:	Proteins, Protein Conformation, Time Factors, Software
Depositing User:	Symplectic Admin
Date Deposited:	29 Jan 2015 10:22
Last Modified:	15 Dec 2022 15:53
DOI:	10.1107/S1399004714025784
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/2002680