MULTIWAVELENGTH XRAY ANAL OF GENE V PROTEIN CRYSTALS CONTAINING SELENOMETHIONINE

基因V蛋白是由F1噬菌体产生的 感染了大肠杆菌。这种蛋白质与病毒DNA结合，呈环状。 并监管超级卷绕。这两个国家之间存在冲突 以前发表的结构和二维核磁共振分析的结果。 改进的结构将极大地便利对 点突变的研究结果和基因的测定 它们的结构通过分子置换。1992年，我们收集了 来自晶体的MAD数据，其中蛋氨酸被替换为 硒蛋氨酸。现在已经确定了2.5E的X射线结构 分辨率通过MAD阶段化，并已在1.8E的分辨率下进行了细化 利用天然基因V蛋白X-射线数据，R因子为19.2%。这个 结构类似于先前发表的x射线结构 基因V蛋白，但在链的比对上不同 B-结构。

The gene V protein is produced by the f1 bacteriophage which infects E. coli. The protein binds to the viral DNA which is circular and regulates supercoiling. There is a conflict between the previously published structure and the results of 2-D NMR analysis. An improved structure would greatly facilitate the interpretation of the results of studies of point mutations and the determination of their structures through molecular replacement. In 1992, we collected MAD data from crystals in which the methionines had been replaced with selenomethionine. The x-ray structure has now been determined at 2.5E resolution by MAD phasing and has been refined at a resolution of 1.8E with an R-factor of 19.2% using native gene V protein x-ray data. The structure is similar to a previously published x-ray structure for gene V protein, but differs in the alignment of strands of b-structure.