Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models.
Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models.
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DOI：
10.1107/s1399004714025784
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发表时间：
2015-02
期刊：
影响因子：
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通讯作者：
Rigden DJ
中科院分区：
文献类型：
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作者：
Keegan RM;Bibby J;Thomas J;Xu D;Zhang Y;Mayans O;Winn MD;Rigden DJ
两个从头算建模程序解决了互补的靶点集，提高了大量小蛋白质的成功。大量的簇和截断从头算蛋白质结构预测，为分子替换产生搜索模型。这里显示了使用不同从头计算模拟程序夸克和罗塞塔求解的目标之间有趣的互补性程度。从任一程序派生的搜索模型共同解决了测试集中几乎所有的全螺旋目标。PHASER仅在5 分钟后产生的初始溶液表现得出人意料地好，在同步加速器访问期间充分改善了原位结构溶液的前景。综上所述，这些结果表明，Sundant有可能比之前怀疑的更快、更成功地解决更多目标。
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.