Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models
- STFC Rutherford Appleton Laboratory, Didcot OX11 0FA (United Kingdom)
- University of Liverpool, Liverpool L69 7ZB (United Kingdom)
- Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037 (United States)
- University of Michigan, Ann Arbor, MI 48109 (United States)
- Science and Technology Facilities Council Daresbury Laboratory, Warrington WA4 4AD (United Kingdom)
Two ab initio modelling programs solve complementary sets of targets, enhancing the success of AMPLE with small proteins. 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.
- OSTI ID:
- 22347711
- Journal Information:
- Acta Crystallographica. Section D: Biological Crystallography, Vol. 71, Issue Pt 2; Other Information: PMCID: PMC4321487; PMID: 25664744; PUBLISHER-ID: rr5080; OAI: oai:pubmedcentral.nih.gov:4321487; Copyright (c) Keegan et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0907-4449
- Country of Publication:
- Denmark
- Language:
- English
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