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|Title:||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.|
|Citation:||ACTA CRYSTALLOGR SECT F STRUCT BIOL CRYST COMMUN, 2011, 67 (Pt 1), pp. 72-75|
|Abstract:||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 I4(1)22, 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.|
|Appears in Collections:||Published Articles, Dept. of Biochemistry|
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