Publikation: Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models
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2015
Autor:innen
Keegan, Ronan M.
Bibby, Jaclyn
Thomas, Jens
Xu, Dong
Zhang, Yang
Winn, Martyn D.
Rigden, Daniel J.
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Acta Crystallographica Section D Biological Crystallography. 2015, 71(2), pp. 338-343. ISSN 0907-4449. eISSN 1399-0047. Available under: doi: 10.1107/S1399004714025784
Zusammenfassung
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.
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570 Biowissenschaften, Biologie
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KEEGAN, Ronan M., Jaclyn BIBBY, Jens THOMAS, Dong XU, Yang ZHANG, Olga MAYANS, Martyn D. WINN, Daniel J. RIGDEN, 2015. Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models. In: Acta Crystallographica Section D Biological Crystallography. 2015, 71(2), pp. 338-343. ISSN 0907-4449. eISSN 1399-0047. Available under: doi: 10.1107/S1399004714025784BibTex
@article{Keegan2015-02-01Explo-34959,
year={2015},
doi={10.1107/S1399004714025784},
title={Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models},
number={2},
volume={71},
issn={0907-4449},
journal={Acta Crystallographica Section D Biological Crystallography},
pages={338--343},
author={Keegan, Ronan M. and Bibby, Jaclyn and Thomas, Jens and Xu, Dong and Zhang, Yang and Mayans, Olga and Winn, Martyn D. and Rigden, Daniel J.}
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<dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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