期刊
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
卷 56, 期 -, 页码 520-523出版社
MUNKSGAARD INT PUBL LTD
DOI: 10.1107/S0907444900000299
关键词
-
A data set from the serine protease porcine pancreatic elastase was collected at atomic resolution (1.1 Angstrom) with synchrotron radiation. The improved resolution allows the determination of atom positions with high accuracy, as well as the localization of H atoms. Three residues could be modelled in alternative positions. The catalytic triad of elastase consists of His57, Asp102 and Ser195. The His57 N-delta 1 H atom was located at a distance of 0.82 Angstrom from the N-delta 1 atom. The distance between His57 N-delta 1 and Asp102 O-delta 2 is 2.70 +/- 0.04 Angstrom, thus indicating normal hydrogen-bonding geometry. Additional H atoms at His57 N-epsilon 2 and Ser195 O-gamma could not be identified in the F-o - F-c density maps.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据