CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC DATA ON ESCHERICHIA-COLI TEM1 BETA-LACTAMASE

被引：16

作者：

JELSCH, C

LENFANT, F

MASSON, JM

SAMAMA, JP

机构：

[1] INST BIOL MOLEC & CELLULAIRE, CRISTALLOG BIOL LAB, 15 RUE RENE DESCARTES, F-67084 STRASBOURG, FRANCE

[2] CNRS, UA 544, INST NATL SCI APPL, CTR TRANSFERT BIOTECHNOL & MICROBIOL, F-31400 TOULOUSE, FRANCE

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 223卷 / 01期

关键词：

CRYSTALLIZATION; BETA-LACTAMASE; ESCHERICHIA-COLI TEM1; ANTIBIOTICS; X-RAY STRUCTURE;

D O I：

10.1016/0022-2836(92)90739-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two crystal forms of Gram- bacteria TEM β-lactamase have been obtained. The tetragonal form has a very large unit cell and diffracts to 3·0 Å resolution. Orthorhombic crystals, grown using ammonium sulfate and a small amount of acetone as precipitating agents, belong to space group P212121 with cell parameters a = 43·1 A ̊, b = 64·4 A ̊, c = 91·2 a ̊ and diffract to 1·7 Å resolution. A seeding procedure has been designed that ensures reproducibility of the crystal properties. Molecular replacement, using a model reconstructed from the Cα co-ordinates from Staphylococcus aureus PC1 β-lactamase, gives a solution that satisfies crystal packing constraints. © 1992.

引用

页码：377 / 380

页数：4

共 28 条

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