Crystallization and preliminary crystallographic study of a component of the Escherichia coli Tol system: TolB

被引：7

作者：

Abergel, C

Rigal, A

Chenivesse, S

Lazdunski, C

Claverie, JM

Bouveret, E

Benedetti, H

机构：

[1] Inst Biol Struct & Microbiol, F-13402 Marseille 20, France

[2] Inst Biol Struct & Microbiol, Lab Ingn & Dynam Syst Membranaires, UPR 9027, F-13402 Marseille 20, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1998年 / 54卷

关键词：

D O I：

10.1107/S0907444997008020

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

TolB from Escherichia coli is part of the Tol system used by the group A colicins to penetrate and kill cells. A TolB derivative tagged with six histidines was overexpressed, purified by chelation on a nickel affinity column and crystallized using the SAmBA software to define the optimal crystallization protocol. The crystals belong to the monoclinic system, space group P2(1) with unit-cell parameters a = 64.48, b = 41.06, c = 78.41 Angstrom, beta = 110.78 degrees. Frozen crystals diffract to 1.9 Angstrom resolution. Screening for heavy-atom derivatives both on the native TolB and various cysteine-substituted mutants is in progress. In addition, a selenomethionine-substituted protein is being produced in order to use the MAD method for structure determination.

引用

页码：102 / 104

页数：3

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