灰色链霉菌氨肽酶的结晶及初步晶体学分析
Crystallization and preliminary crystallographic analysis of Streptomyces griseus aminopeptidase.
作者信息
Almog O, Greenblatt H M, Spungin A, Ben-Meir D, Blumberg S, Shoham G
机构信息
Department of Inorganic Chemistry, Hebrew University of Jerusalem, Israel.
出版信息
J Mol Biol. 1993 Mar 5;230(1):342-4. doi: 10.1006/jmbi.1993.1146.
Streptomyces griseus excretes a small molecular mass (30 kDa) aminopeptidase that could be used for various biotechnological applications. This enzyme was isolated from an extracellular protease mixture of Streptomyces griseus (Pronase E. Sigma) and single crystals were obtained by the vapor diffusion method using polyethylene glycol 4000 as the precipitant. The crystals belong to the tetragonal space group P4(1)2(1)2 (P4(3)2(1)2), with cell dimensions of a = b = 61.82(3) A and c = 145.88(4) A. These crystals are mechanically strong, they are stable in the X-ray beam and they diffract to better than 1.8 A resolution. The cell dimensions and the cell symmetry are consistent with one molecule in the asymmetric unit and the crystals are suitable for a detailed high-resolution crystallographic analysis. A complete native data set to 1.9 A resolution has been collected on a Rigaku R-AXIS-IIC Imaging Plate Detector system and a heavy-atom derivative search is in progress.
灰色链霉菌分泌一种小分子质量（30 kDa）的氨肽酶，可用于各种生物技术应用。该酶从灰色链霉菌的细胞外蛋白酶混合物（链霉蛋白酶E. Sigma）中分离得到，通过气相扩散法以聚乙二醇4000作为沉淀剂获得了单晶。这些晶体属于四方晶系空间群P4(1)2(1)2（P4(3)2(1)2），晶胞参数为a = b = 61.82(3) Å，c = 145.88(4) Å。这些晶体机械强度高，在X射线束中稳定，衍射分辨率优于1.8 Å。晶胞尺寸和晶胞对称性与不对称单元中的一个分子一致，这些晶体适合进行详细的高分辨率晶体学分析。已在Rigaku R-AXIS-IIC成像板探测器系统上收集了分辨率为1.9 Å的完整天然数据集，重原子衍生物搜索正在进行中。
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