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Expression, purification, crystallization and preliminary X‐ray analysis of wild‐type and of an active‐site mutant of glyceraldehyde‐3‐phosphate dehydrogenase from Campylobacter jejuni

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The genome of the enteric pathogen Campylobacter jejuni encodes a single glyceraldehyde‐3‐phosphate dehydrogenase that can utilize either NADP+ or NAD+ as coenzymes for the oxidative phosphorylation of glyceraldehyde‐3‐phosphate to 1,3‐diphosphoglycerate. Here, the cloning, expression, purification, crystallization and preliminary X‐ray analysis of both the wild type and an active‐site mutant of the enzyme are presented. Preliminary X‐ray analysis revealed that in both cases the crystals diffracted to beyond 1.9 Å resolution. The space group is shown to be I4122, with unit‐cell parameters a = 90.75, b = 90.75, c = 225.48 Å, α = 90.46, β = 90.46, γ = 222.79°; each asymmetric unit contains only one subunit of the tetrameric enzyme.
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Keywords: Campylobacter jejuni; glyceraldehyde‐3‐phosphate dehydrogenase

Document Type: Research Article

Affiliations: Henry Wellcome Laboratories for Structural Biology, Henry Wellcome Building, University of Leicester, Leicester LE1 9HN, England

Publication date: January 1, 2011

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