大肠杆菌TEM1β-内酰胺酶的结晶及初步晶体学数据

Crystallization and preliminary crystallographic data on Escherichia coli TEM1 beta-lactamase.

作者信息

Jelsch C, Lenfant F, Masson J M, Samama J P

机构信息

Laboratoire de Cristallographie Biologique IBMC, 67084 Strasbourg, France.

出版信息

J Mol Biol. 1992 Jan 5;223(1):377-80. doi: 10.1016/0022-2836(92)90739-7.

DOI:10.1016/0022-2836(92)90739-7

PMID:1731083

Abstract

Two crystal forms of Gram- bacteria TEM beta-lactamase have been obtained. The tetragonal form has a very large unit cell and diffracts to 3.0 A resolution. Orthorhombic crystals, grown using ammonium sulfate and a small amount of acetone as precipitating agents, belong to space group P2(1)2(1)2(1) with cell parameters a = 43.1 A, b = 64.4 A, c = 91.2 A and diffract to 1.7 A resolution. A seeding procedure has been designed that ensures reproducibility of the crystal properties. Molecular replacement, using a model reconstructed from the C alpha co-ordinates from Staphylococcus aureus PC1 beta-lactamase, gives a solution that satisfies crystal packing constraints.

摘要

已获得革兰氏阴性菌TEMβ-内酰胺酶的两种晶体形式。四方晶型具有非常大的晶胞，衍射分辨率为3.0埃。使用硫酸铵和少量丙酮作为沉淀剂生长的正交晶体属于空间群P2(1)2(1)2(1)，晶胞参数a = 43.1埃，b = 64.4埃，c = 91.2埃，衍射分辨率为1.7埃。设计了一种接种程序，可确保晶体性质的可重复性。使用从金黄色葡萄球菌PC1β-内酰胺酶的Cα坐标重建的模型进行分子置换，得到了一个满足晶体堆积限制的解决方案。