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• W2807631690 abstract "Molecular replacement (MR) has commonly been employed to derive the phase information in protein crystal X-ray diffraction, but its success rate decreases rapidly when the search model is dissimilar to the target. MR-REX has been developed to perform an MR search by replica-exchange Monte Carlo simulations, which enables cooperative rotation and translation searches and simultaneous clash and occupancy optimization. MR-REX was tested on a set of 1303 protein structures of different accuracies and successfully placed 699 structures at positions that have an r.m.s.d. of below 2 Å to the target position, which is 10% higher than was obtained by Phaser . However, cases studies show that many of the models for which Phaser failed and MR-REX succeeded can be solved by Phaser by pruning them and using nondefault parameters. The factors effecting success and the parts of the methodology which lead to success are studied. The results demonstrate a new avenue for molecular replacement which outperforms (and has results that are complementary to) the state-of-the-art MR methods, in particular for distantly homologous proteins." @default.
• W2807631690 created "2018-06-13" @default.
• W2807631690 creator A5022802322 @default.
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• W2807631690 date "2018-06-08" @default.
• W2807631690 modified "2023-10-17" @default.
• W2807631690 title "<i>MR-REX</i>: molecular replacement by cooperative conformational search and occupancy optimization on low-accuracy protein models" @default.
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• W2807631690 doi "https://doi.org/10.1107/s2059798318005612" @default.
• W2807631690 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6038387" @default.
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