Postma J P, Parker M W, Tsernoglou D
European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
Acta Crystallogr A. 1989 Jul 1;45 ( Pt 7):471-7. doi: 10.1107/s0108767389002552.
Crystallographic refinement based on molecular dynamics (MD) has been applied to a 2.5 A resolution X-ray structure of the pore-forming fragment of colicin A. The crystallographic R factor was reduced from 48 to 23% with a concomitant improvement in stereochemical parameters. The method considerably speeded up the refinement process but was associated with some pitfalls. In particular, some badly fitted segments of the structure required manual rebuilding, even after MD refinement and some problems with weighting schemes were encountered. Analysis of the effects of the refinement and ideas for improvements are presented.
基于分子动力学（MD）的晶体学精修已应用于大肠杆菌素A成孔片段分辨率为2.5埃的X射线结构。晶体学R因子从48%降至23%，同时立体化学参数得到改善。该方法显著加快了精修过程，但也存在一些缺陷。特别是，即使经过MD精修，结构中一些拟合不佳的片段仍需要人工重建，并且遇到了一些加权方案的问题。本文介绍了精修效果分析及改进思路。
