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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 12(66), p. 1579-1582, 2010

DOI: 10.1107/s1744309110026606

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Crystallization and preliminary X-ray analysis of a novel esterase Rv0045c fromMycobacterium tuberculosis

Journal article published in 2010 by Lipeng Xu, Jiubiao Guo, Xiangdong Zheng, Tingyi Wen ORCID, Fei Sun, Siguo Liu, Hai Pang
This paper is available in a repository.
This paper is available in a repository.

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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, α=β=90, γ=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.