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Crystallization and preliminary X-ray analysis of a novel esterase Rv0045c from Mycobacterium tuberculosis.

ABSTRACT: The Rv0045c protein is predicted to be an esterase that is involved in lipid metabolism in Mycobacterium tuberculosis. The protein was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The Rv0045c protein crystals diffracted to a resolution of 2.7?Å using a synchrotron-radiation source and belonged to space group P3(1) or P3(2), with unit-cell parameters a=b=73.465, c=48.064?Å, ?=?=90, ?=120°. Purified SeMet-labelled Rv0045c protein was also crystallized and formed crystals that diffracted to a resolution of 3.0?Å using an in-house X-ray radiation source.

SUBMITTER: Xu L

PROVIDER: S-EPMC2998358 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of a novel esterase Rv0045c from Mycobacterium tuberculosis.

Xu Lipeng L Guo Jiubiao J Zheng Xiangdong X Wen Tingyi T Sun Fei F Liu Siguo S Pang Hai H

Acta crystallographica. Section F, Structural biology and crystallization communications 20101116 Pt 12

The Rv0045c protein is predicted to be an esterase that is involved in lipid metabolism in Mycobacterium tuberculosis. The protein was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The Rv0045c protein crystals diffracted to a resolution of 2.7 Å using a synchrotron-radiation source and belonged to space group P3(1) or P3(2), with unit-cell parameters a=b=73.465, c=48.064 Å, α=β=90, γ=120°. Purified SeMet-labelled Rv0045c protein was a ...[more]

PMID: 21139199

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