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