Crystal engineering:: a case study using the 24 kDa fragment of the DNA gyrase B subunit from Escherichia coli

被引：40

作者：

D'Arcy, A ^{[1
]}

Stihle, M ^{[1
]}

Kostrewa, D ^{[1
]}

Dale, G ^{[1
]}

机构：

[1] F Hoffmann La Roche Ltd, Pharmaceut Res, Chem Technol, CH-4070 Basel, Switzerland

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷

关键词：

D O I：

10.1107/S0907444999008136

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Site-directed mutagenesis was used to determine the efficacy of changing surface residues to improve crystal quality. Nine mutants of the 24 kDa fragment of the Escherichia coli DNA gyrase B subunit were produced, changing residues on the protein's surface. The mutations changed either the charge or the polarity of the wild-type amino acid. It was found that single amino-acid changes on the surface could have a dramatic effect on the crystallization properties of the protein and generally resulted in an improvement in the number of crystal-screen hits as well as an improvement in crystal quality. It is concluded that crystal engineering is a valuable tool for protein crystallography.

引用

页码：1623 / 1625

页数：3

共 11 条

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