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Cloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of the small subunit of isopropylmalate isomerase (Rv2987c) from Mycobacterium tuberculosis

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Two C‐terminally truncated variants of the small subunit of Mycobacterium tuberculosis isopropylmalate isomerase (Rv2987c; LeuD), LeuD_1‐156 and LeuD_1‐168, have been cloned, heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized. The crystals of LeuD_1‐156 belonged to the hexagonal system (space group P6122 or P6522) with up to four subunits in the asymmetric unit, whereas the crystals of LeuD_1‐168 belonged to the monoclinic system (space group P21) with two subunits in the asymmetric unit. Both crystals diffracted X‐rays to beyond 2.0 Å resolution and were suitable for further crystallographic analysis.
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Keywords: Mycobacterium tuberculosis; Rv2987c; isopropylmalate isomerase

Document Type: Research Article

Publication date: February 1, 2009

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