Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/110744/1/S1399004714025784.pd

Bibby, Jaclyn

Keegan, Ronan M.

Mayans, Olga

Rigden, Daniel J.

Thomas, Jens

Winn, Martyn D.

Xu, Dong

Zhang, Yang

Acta Crystallographica Section D Biological Crystallography

PubMed

AMPLEclusters and truncatesab initioprotein structure predictions, producing search models for molecular replacement. Here, an interesting degree of complementarity is shown between targets solved using the differentab initiomodelling programsQUARKandROSETTA. Search models derived from either program collectively solve almost all of the all-helical targets in the test set. Initial solutions produced byPhaserafter only 5 min perform surprisingly well, improving the prospects forin situstructure solution byAMPLEduring synchrotron visits. Taken together, the results show the potential forAMPLEto run more quickly and successfully solve more targets than previously suspected.</jats:p

Ronan M. Keegan

Jaclyn Bibby

Jens Thomas

Dong Xu

Yang Zhang

Olga Mayans

Martyn D. Winn

Daniel J. Rigden

Crossref

Exploring the speed and performance of molecular replacement withAMPLEusingQUARK ab initioprotein models

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.publishe

KOPS - The Institutional Repository of the University of Konstanz

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

Deep Blue Documents

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

Keegan, Ronan M

Winn, Martyn D

Rigden, Daniel J

University of Liverpool Repository

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

Konstanzer Online-Publikations-System

http://creativecommons.org/licenses/by/2.0/uk/

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

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Crossref

KOPS - The Institutional Repository of the University of Konstanz

Deep Blue Documents

University of Liverpool Repository

Konstanzer Online-Publikations-System