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Molecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction studies of histidinol phosphate aminotransferase (HisC2) from Mycobacterium tuberculosis
Nazia Nasir, , Chetna Chugh, Mohammad Ahangar Syed, Bichitra Biswal K.
Published in
Volume: 68
Issue: 1
Pages: 32 - 36
HisC2 from Mycobacterium tuberculosis was overexpressed in M. smegmatis and purified to homogeneity using nickel-nitrilotriacetic acid metal-affinity and gel-filtration chromatography. Diffraction-quality crystals were grown using the hanging-drop vapour-diffusion technique from a condition consisting of 7 mg ml-1 HisC2 (in 20 mM Tris pH 8.8, 50 mM NaCl and 5% glycerol), 1 M succinic acid pH 7.0, 0.1 M HEPES pH 7.0 and 1%(w/v) polyethylene glycol monomethyl ether 2000. The crystals belonged to the orthorhombic space group P21212, with unit-cell parameters a = 255.98, b = 77.09, c = 117.97 {\AA}. X-ray diffraction data were recorded to 2.45 {\AA} resolution from a single crystal using the in-house X-ray facility. {\textcopyright} 2012 International Union of Crystallography. All rights reserved.
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