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. 1998 Jan 1;54(Pt 1):102-4.
doi: 10.1107/s0907444997008020.

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

C Abergel  1 , A Rigal, S Chenivesse, C Lazdunski, J M Claverie, E Bouveret, H Bénédetti
Affiliations

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

C Abergel et al. Acta Crystallogr D Biol Crystallogr. .

Abstract

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 P21 with unit-cell parameters a = 64.48, b = 41.06, c = 78.41 A, beta = 110.78 degrees. Frozen crystals diffract to 1.9 A 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.

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