Please use this identifier to cite or link to this item:
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.
Authors: Tourigny, DS
Elliott, PR
Edgell, LJ
Hudson, GM
Moody, PC
First Published: 1-Jan-2011
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.
DOI Link: 10.1107/S1744309110044465
eISSN: 1744-3091
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

Files in This Item:
There are no files associated with this item.

Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.