蛋白酶抑制剂依科汀的结晶及初步X射线晶体学分析

Crystallization and preliminary X-ray crystallographic analysis of the protease inhibitor ecotin.

作者信息

Shin D H, Hwang K Y, Kim K K, Lee H R, Lee C S, Chung C H, Suh S W

机构信息

Department of Chemistry, College of Natural Sciences, Seoul National University, Korea.

出版信息

J Mol Biol. 1993 Feb 20;229(4):1157-8. doi: 10.1006/jmbi.1993.1112.

DOI:10.1006/jmbi.1993.1112

PMID:8445642

Abstract

Ecotin, a novel serine protease inhibitor isolated from Escherichia coli, has been crystallized using polyethylene glycol 1500 as the precipitating agent. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters of a = 39.22 A, b = 84.86 A, and c = 98.74 A. The asymmetric unit contains one dimeric molecule of ecotin, with a crystal volume per protein mass (Vm) of 2.55 A3/Da and a solvent content of 51.8% by volume. The crystals diffract to at least 2.2 A using a conventional X-ray source, and X-ray data have been collected to 2.7 A Bragg spacing from a native crystal.

摘要

埃考汀是一种从大肠杆菌中分离出的新型丝氨酸蛋白酶抑制剂，已使用聚乙二醇1500作为沉淀剂进行结晶。晶体属于正交晶系空间群P2(1)2(1)2(1)，晶胞参数为a = 39.22 Å，b = 84.86 Å，c = 98.74 Å。不对称单元包含一个埃考汀二聚体分子，每蛋白质质量的晶体体积（Vm）为2.55 Å³/Da，溶剂含量为51.8%（体积）。使用传统X射线源，晶体衍射至至少2.2 Å，并且已从天然晶体收集到布拉格间距为2.7 Å的X射线数据。