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

Horsham, M., Saxby, H., Blake, J., Isaacs, N., Mitchell, T.J. and Riboldi-Tunnicliffe, A. (2010) Expression, purification, crystallization and preliminary X-ray crystallographic data from TktA, a transketolase from the lactic acid bacteriumLactobacillus salivarius. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 66(8), pp. 899-901. (doi: 10.1107/S1744309110012157)

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Publisher's URL: http://dx.doi.org/10.1107/S1744309110012157

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 P3221, with unit-cell parameters a = b = 75.43, c = 184.11 Å, and showed diffraction to 2.3 Å resolution.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Riboldi-Tunnicliffe, Dr Alan and Isaacs, Professor Neil and Mitchell, Professor Timothy
Authors: Horsham, M., Saxby, H., Blake, J., Isaacs, N., Mitchell, T.J., and Riboldi-Tunnicliffe, A.
College/School:College of Science and Engineering > School of Chemistry
College of Medical Veterinary and Life Sciences > School of Infection & Immunity
Journal Name:Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
Publisher:Wiley-Blackwell Publishing, Inc.
ISSN:1744-3091
ISSN (Online):1744-3091

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