title: Sample preparation, crystallization and structure solution of HisC from Mycobacterium tuberculosis.
abstract: Histidinolphosphate aminotransferase (HisC; Rv1600) 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 suitable for X-ray analysis were grown by the hanging-drop vapour-diffusion technique using 30% polyethylene glycol monomethyl ether 2000 as the precipitant. The crystals belonged to the hexagonal space group P3221, with an unusual high solvent content of 74.5%. X-ray diffraction data were recorded to 3.08 Å resolution from a single crystal using in-house Cu Kα radiation. The structure of HisC was solved by the molecular-replacement method using its Corynebacterium glutamicum counterpart as a search model. HisC is a dimer in the crystal as well as in solution.
authors.affiliation: Protein Crystallography Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110 067, India.
authors.forename: Nazia
authors.initials: N
authors.lastname: Nasir
authors.forename: Rajan
authors.initials: R
authors.lastname: Vyas
authors.forename: Bichitra K
authors.initials: BK
authors.lastname: Biswal
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006641:Histidinol / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D010710:Phosphates / Q000378:metabolism; D000637:Transaminases / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D010710:Phosphates; D006641:Histidinol; D000637:Transaminases
keywords: HisC; Mycobacterium tuberculosis; Rv1600; histidinolphosphate aminotransferase
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