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

Chantal Abergel (1) , A Rigal , S Chenivesse , C Lazdunski , J.M Claverie , E. Bouveret , H Bénédetti (2)

1 IGS - Information génomique et structurale
2 LISM - Laboratoire d'ingénierie des systèmes macromoléculaires

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.

Domaines: Sciences du Vivant [q-bio]

Chantal Abergel, A Rigal, S Chenivesse, C Lazdunski, J.M Claverie, et al.. Crystallization and preliminary crystallographic study of a component of the Escherichia coli tol system: TolB.. Acta crystallographica Section D : Structural biology [1993-..], 1998, 54 (Pt 1), pp.102-4. ⟨hal-02130160⟩