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Expression, purification, crystallization and preliminary X-ray studies of Vibrio cholerae pseudopilin EpsH.


ABSTRACT: EpsH is a minor pseudopilin protein of the Vibrio cholerae type II secretion system. A truncated form of EpsH with a C-terminal noncleavable His tag was constructed and expressed in Escherichia coli, purified and crystallized by sitting-drop vapor diffusion. A complete data set was collected to 1.71 A resolution. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.39, b = 71.11, c = 84.64 A. There were two protein molecules in the asymmetric unit, which gave a Matthews coefficient V(M) of 2.1 A(3) Da(-1), corresponding to 41.5% solvent content.

SUBMITTER: Raghunathan K 

PROVIDER: S-EPMC2705639 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray studies of Vibrio cholerae pseudopilin EpsH.

Raghunathan Kannan K   Vago Frank S FS   Ball Terry T   Yakubova Nafissa N   Grindem David D   Wedemeyer William J WJ   Arvidson Dennis N DN  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090627 Pt 7


EpsH is a minor pseudopilin protein of the Vibrio cholerae type II secretion system. A truncated form of EpsH with a C-terminal noncleavable His tag was constructed and expressed in Escherichia coli, purified and crystallized by sitting-drop vapor diffusion. A complete data set was collected to 1.71 A resolution. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.39, b = 71.11, c = 84.64 A. There were two protein molecules in the asymmetric unit, which gave a Ma  ...[more]

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