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Expression, purification, crystallization and preliminary X-ray studies of Lactobacillus jensenii enolase.

ABSTRACT: Recombinant Lactobacillus jensenii enolase fused to a C-terminal noncleavable His tag was expressed in Escherichia coli, purified and crystallized by sitting-drop vapor diffusion. A complete data set was collected to 3.25 A resolution. The crystals belonged to space group I4, with unit-cell parameters a=b=145.31, c=99.79 A. There were two protein subunits in the asymmetric unit, which gave a Matthews coefficient VM of 2.8 A3 Da(-1), corresponding to 55.2% solvent content.

SUBMITTER: Harris PT

PROVIDER: S-EPMC2917297 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray studies of Lactobacillus jensenii enolase.

Harris Paul T PT Raghunathan Kannan K Spurbeck Rachel R RR Arvidson Cindy G CG Arvidson Dennis N DN

Acta crystallographica. Section F, Structural biology and crystallization communications 20100729 Pt 8

Recombinant Lactobacillus jensenii enolase fused to a C-terminal noncleavable His tag was expressed in Escherichia coli, purified and crystallized by sitting-drop vapor diffusion. A complete data set was collected to 3.25 A resolution. The crystals belonged to space group I4, with unit-cell parameters a=b=145.31, c=99.79 A. There were two protein subunits in the asymmetric unit, which gave a Matthews coefficient VM of 2.8 A3 Da(-1), corresponding to 55.2% solvent content. ...[more]

PMID: 20693674

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