Thorn Andrea, Sheldrick George M
Department of Haematology, University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, England.
Acta Crystallogr D Biol Crystallogr. 2013 Nov;69(Pt 11):2251-6. doi: 10.1107/S0907444913027534. Epub 2013 Oct 18.
Although the program SHELXE was originally intended for the experimental phasing of macromolecules, it can also prove useful for expanding a small protein fragment to an almost complete polyalanine trace of the structure, given a favourable combination of native data resolution (better than about 2.1 Å) and solvent content. A correlation coefficient (CC) of more than 25% between the native structure factors and those calculated from the polyalanine trace appears to be a reliable indicator of success and has already been exploited in a number of pipelines. Here, a more detailed account of this usage of SHELXE for molecular-replacement solutions is given.
尽管SHELXE程序最初是用于大分子的实验相位分析，但如果天然数据分辨率（优于约2.1 Å）和溶剂含量的组合有利，它也可用于将小的蛋白质片段扩展为几乎完整的结构聚丙氨酸迹线。天然结构因子与从聚丙氨酸迹线计算出的结构因子之间的相关系数（CC）超过25%似乎是成功的可靠指标，并且已经在许多流程中得到应用。在此，给出了关于SHELXE在分子置换解决方案中的这种用法的更详细说明。
