Chapman M S, Rossmann M G
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA.
Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):129-42. doi: 10.1107/S0907444995007268.
The canine parvovirus structure (CPV) [Tsao, Chapman, Agbandje, Keller, Smith, Wu, Luo, Smith, Rossmann, Compans & Parrish (1991). Science, 251, 1456-1464] has been refined by a real-space refinement procedure [Chapman (1994). Acta Cryst. A51, 69-801. The fit of an atomic model to electron density was optimized while taking into account the resolution limit of the data and the stereochemistry of the structure. The refined model had a reasonable free R factor [Brtinger (1992). Nature (London), 355, 472-4751 of 0.29. The method is particularly fast and convenient when only a small fraction of the crystallographic asymmetric unit needs to be refined, as is the case when there is high non-crystallographic redundancy. Cycles of refinement for virus capsids were completed in about 1/50th of the time required for equivalent reciprocal-space procedures.
犬细小病毒结构(CPV)[曹、查普曼、阿班德杰、凯勒、史密斯、吴、罗、史密斯、罗斯曼、康潘斯和帕里什(1991年)。《科学》,251卷,第1456 - 1464页]已通过实空间精修程序[查普曼(1994年)。《晶体学报》A51卷,第69 - 801页]进行了精修。在考虑数据分辨率极限和结构立体化学的同时,优化了原子模型与电子密度的拟合。精修后的模型具有合理的自由R因子[布林格(1992年)。《自然》(伦敦),355卷,第472 - 475页],为0.29。当仅需精修晶体学不对称单元的一小部分时,该方法特别快速且方便,在存在高非晶体学冗余的情况下就是如此。病毒衣壳的精修循环大约在等效倒易空间程序所需时间的1/50内完成。