CRYSTALLOGRAPHIC REFINEMENT BY SIMULATED ANNEALING APPLICATION TO A 2.8-A RESOLUTION STRUCTURE OF ASPARTATE-AMINOTRANSFERASE
CRYSTALLOGRAPHIC REFINEMENT BY SIMULATED ANNEALING APPLICATION TO A 2.8-A RESOLUTION STRUCTURE OF ASPARTATE-AMINOTRANSFERASE
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DOI：
10.1016/0022-2836(88)90211-2
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发表时间：
1988-10-05
影响因子：
5.6
通讯作者：
BRUNGER, AT
中科院分区：
文献类型：
--
作者：
BRUNGER, AT
利用分子动力学通过模拟退火进行的晶体学细化已经应用于2.8埃。（1. = 0.1nm）分辨率的天冬氨酸转氨酶的X射线结构。比较的精制结构和结构得到的组合约束最小二乘细化和手动重新拟合显示出类似的R因子，立体化学，和平均差异的同晶置换相质心。通过模拟退火进行的晶体学细化实现了结构变化和电子密度图的改进，而这是使用不需要手动重新拟合的约束最小二乘细化无法实现的。通过模拟退火的晶体学精修可以产生一系列结构，其中每个结构都与衍射信息一致。大的整体变化的区域表明错误地拟合或无序的大分子片段。
Crystallographic refinement by simulated annealing with molecular dynamics has been applied to a 2.8 .ANG. (1 .ANG. = 0.1nm) resolution X-ray structure of aspartate aminotransferase. Comparison of the refined structure and a structure obtained by combined restrained least-squares refinement and manual re-fitting shows a similar R factor, stereochemistry, and mean difference from the isomorphous replacement phase centroids. Crystallographic refinement by simulated annealing accomplished structural changes and improvements of the electron density maps that were not possible by using restrained least-squares refinement without manual re-fitting. Crystallographic refinement by simulated annealing can generate an ensemble of structures, each of which agrees with the diffraction information. Regions of large variations of the ensemble indicate either erroneously fitted or disorded segments of the macromolecule.