Expression, purification, crystallization and preliminary X-ray crystallographic data from TktA, a transketolase from the lactic acid bacterium Lactobacillus salivarius.
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.
Horsham
Matt
M
FBLS I&I, University of Glasgow, 120 University Place, Glasgow G12 8TA, Scotland.
Saxby
Harriet
H
Blake
James
J
Isaacs
Neil W
NW
Mitchell
Tim J
TJ
Riboldi-Tunnicliffe
Alan
A
D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D007778:Lactobacillus / Q000201:enzymology*; D014174:Transketolase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D014174:Transketolase