REFINED CRYSTAL-STRUCTURE OF BOVINE BETA-TRYPSIN AT 1.8 A RESOLUTION .1. CRYSTALLIZATION, DATA-COLLECTION AND APPLICATION OF PATTERSON SEARCH TECHNIQUES
REFINED CRYSTAL-STRUCTURE OF BOVINE BETA-TRYPSIN AT 1.8 A RESOLUTION .1. CRYSTALLIZATION, DATA-COLLECTION AND APPLICATION OF PATTERSON SEARCH TECHNIQUES
复制标题
DOI：
10.1016/s0022-2836(75)80004-0
复制
发表时间：
1975-01-01
影响因子：
5.6
通讯作者：
BODE, W
中科院分区：
文献类型：
--
作者：
FEHLHAMMER, H;BODE, W
在pH7.0的条件下，从苄脒抑制的牛β-胰蛋白酶单晶中收集到了分辨率为1.8 μ m的X射线强度数据。考虑到在牛胰蛋白酶-胰蛋白酶抑制剂复合物的晶体结构中发现的精细原子坐标（Huberet等人，1974），胰蛋白酶分子已经应用Patterson搜索技术定位在胰蛋白酶晶体内。使用最佳取向和位置参数，计算出6.8 - 1.8 μ m分辨率数据的晶体学R因子为0.43。
X-ray intensity data to 1·8 Å resolution have been collected from a single crystal of benzamidine-inhibited bovineβ-trypsin at pH 7·0. Given the refined atomic co-ordinates as found in the crystal structure of bovine trypsin-pancreatic trypsin inhibitor complex (Huberet al., 1974) the trypsin molecules have been located within the trypsin crystals applying Patterson search techniques. Using the optimal orientation and position parameters a crystallographicR-factor of 0·43 was calculated for data from 6·8 to 1·8 Å resolution.