MULTIWAVELENGTH XRAY ANAL OF GENE V PROTEIN CRYSTALS CONTAINING SELENOMETHIONINE

基因V蛋白由f1噬菌体产生， 感染E.杆菌 这种蛋白质与环状的病毒DNA结合 并调节超螺旋。 之间存在冲突 先前公布的结构和2-D NMR分析的结果。 改进后的结构将极大地便利对《公约》的解释， 点突变的研究结果和 它们的结构通过分子置换。 1992年，我们收集了 来自其中甲硫氨酸已被取代的晶体的MAD数据 硒代蛋氨酸。 X射线结构现已确定在2.5E 通过MAD定相的分辨率，并已在1.8E的分辨率下进行了改进 使用天然基因V蛋白X射线数据，R因子为19.2%。 的 结构类似于先前公布的X射线结构， 基因V蛋白，但不同之处在于链的排列， 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.