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

Matt Horsham; Harriet Saxby; James Blake; Neil W Isaacs; Tim J Mitchell; Alan Riboldi-Tunnicliffe

doi:10.1107/S1744309110012157

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

Matt Horsham, Harriet Saxby, James Blake, Neil W Isaacs, Tim J Mitchell, Alan Riboldi-Tunnicliffe

Immunology and Immunotherapy

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1 Citation (Scopus)

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.

Original language	English
Pages (from-to)	899-901
Number of pages	3
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume	66
Issue number	Pt 8
DOIs	https://doi.org/10.1107/S1744309110012157
Publication status	Published - 1 Aug 2010

Keywords

Crystallization
Crystallography, X-Ray
Gene Expression
Lactobacillus
Transketolase

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10.1107/S1744309110012157

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

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

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.",

keywords = "Crystallization, Crystallography, X-Ray, Gene Expression, Lactobacillus, Transketolase",

author = "Matt Horsham and Harriet Saxby and James Blake and Isaacs, {Neil W} and Mitchell, {Tim J} and Alan Riboldi-Tunnicliffe",

year = "2010",

month = aug,

day = "1",

doi = "10.1107/S1744309110012157",

language = "English",

volume = "66",

pages = "899--901",

journal = "Acta Crystallographica Section F Structural Biology and Crystallization Communications",

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publisher = "International Union of Crystallography",

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Horsham, M, Saxby, H, Blake, J, Isaacs, NW, Mitchell, TJ & Riboldi-Tunnicliffe, A 2010, 'Expression, purification, crystallization and preliminary X-ray crystallographic data from TktA, a transketolase from the lactic acid bacterium Lactobacillus salivarius', Acta Crystallographica Section F Structural Biology and Crystallization Communications, vol. 66, no. Pt 8, pp. 899-901. https://doi.org/10.1107/S1744309110012157

Expression, purification, crystallization and preliminary X-ray crystallographic data from TktA, a transketolase from the lactic acid bacterium Lactobacillus salivarius. / Horsham, Matt; Saxby, Harriet; Blake, James et al.
In: Acta Crystallographica Section F Structural Biology and Crystallization Communications, Vol. 66, No. Pt 8, 01.08.2010, p. 899-901.

Research output: Contribution to journal › Article › peer-review

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T1 - Expression, purification, crystallization and preliminary X-ray crystallographic data from TktA, a transketolase from the lactic acid bacterium Lactobacillus salivarius

AU - Horsham, Matt

AU - Saxby, Harriet

AU - Blake, James

AU - Isaacs, Neil W

AU - Mitchell, Tim J

AU - Riboldi-Tunnicliffe, Alan

PY - 2010/8/1

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N2 - 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.

AB - 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.

KW - Crystallization

KW - Crystallography, X-Ray

KW - Gene Expression

KW - Lactobacillus

KW - Transketolase

U2 - 10.1107/S1744309110012157

DO - 10.1107/S1744309110012157

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SN - 1744-3091

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EP - 901

JO - Acta Crystallographica Section F Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F Structural Biology and Crystallization Communications

IS - Pt 8

ER -

Horsham M, Saxby H, Blake J, Isaacs NW, Mitchell TJ, Riboldi-Tunnicliffe A. Expression, purification, crystallization and preliminary X-ray crystallographic data from TktA, a transketolase from the lactic acid bacterium Lactobacillus salivarius. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 2010 Aug 1;66(Pt 8):899-901. doi: 10.1107/S1744309110012157

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

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Keywords

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