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

RM Keegan, J Bibby, J Thomas, D Xu… - … Section D: Biological …, 2015 - journals.iucr.org
RM Keegan, J Bibby, J Thomas, D Xu, Y Zhang, O Mayans, MD Winn, DJ Rigden
Acta Crystallographica Section D: Biological Crystallography, 2015journals.iucr.org
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 …
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.
International Union of Crystallography
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