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Expression, purification, crystallization and preliminary X-ray crystallographic data from TktA, a transketolase from the lactic acid bacterium Lactobacillus salivarius.

Authors :
Horsham M
Saxby H
Blake J
Isaacs NW
Mitchell TJ
Riboldi-Tunnicliffe A
Source :
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2010 Aug 01; Vol. 66 (Pt 8), pp. 899-901. Date of Electronic Publication: 2010 Jul 27.
Publication Year :
2010

Abstract

The enzyme transketolase from the lactic acid bacterium Lactobacillus salivarius (subsp. salivarius UCC118) has been recombinantly expressed and purified using an Escherichia coli expression system. Purified transketolase from L. salivarius has been crystallized using the vapour-diffusion technique. The crystals belonged to the trigonal space group P3(2)21, with unit-cell parameters a=b=75.43, c=184.11 A, and showed diffraction to 2.3 A resolution.

Details

Language :
English
ISSN :
1744-3091
Volume :
66
Issue :
Pt 8
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology and crystallization communications
Publication Type :
Academic Journal
Accession number :
20693662
Full Text :
https://doi.org/10.1107/S1744309110012157