Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA

被引：12

作者：

Nummelin, H

El Tahir, Y

Ollikka, P

Skurnik, M

Goldman, A

机构：

[1] Univ Helsinki, Inst Biotechnol, FIN-00014 Helsinki, Finland

[2] Univ Turku, Dept Med Biochem & Mol Biol, FIN-20520 Turku, Finland

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2002年 / 58卷

关键词：

D O I：

10.1107/S0907444902005231

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A recombinant form of a collagen-binding fragment of Yersinia enterocolitica serotype O:3 adhesin YadA with an N-terminal polyhistidine affinity tag has been produced in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the trigonal space group R3, with unit-cell parameters a = b = 67.05, c = 221.95 Angstrom, and diffract to 1.55 Angstrom resolution on a synchrotron-radiation source.

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页码：1042 / 1044

页数：3

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