title: Crystallization, high-resolution data collection and preliminary crystallographic analysis of Aura virus capsid protease and its complex with dioxane.
abstract: The C-terminal protease domain of capsid protein from Aura virus expressed in a bacterial expression system has been purified to homogeneity and crystallized. Crystals suitable for X-ray diffraction analysis were obtained by the vapour-diffusion method using 0.1 M bis-tris and polyethylene glycol monomethyl ether 2000. Crystals of the C-terminal protease domain of capsid protein in complex with dioxane were also produced and crystal data were obtained. Both crystals belonged to space group C2, with unit-cell parameters a = 79.6, b = 35.2, c = 49.5 Å. High-resolution data sets were collected to a resolution of 1.81 Å for the native protein and 1.98 Å for the complex. Preliminary crystallographic studies suggested the presence of a single molecule in the crystallographic asymmetric unit, with a solvent content of 38.5%.
authors.affiliation: Department of Biotechnology, Indian Institute of Technology, Roorkee, Roorkee 247 667, India.
authors.forename: Megha
authors.initials: M
authors.lastname: Aggarwal
authors.forename: Sonali
authors.initials: S
authors.lastname: Dhindwal
authors.forename: Shivendra
authors.initials: S
authors.lastname: Pratap
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Kuhn
authors.forename: Pravindra
authors.initials: P
authors.lastname: Kumar
authors.forename: Shailly
authors.initials: S
authors.lastname: Tomar
mesh_terms: D000524:Alphavirus / Q000201:enzymology*; D002213:Capsid / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004146:Dioxanes / Q000737:chemistry* / Q000378:metabolism; D010447:Peptide Hydrolases / Q000737:chemistry*
chemical_list: D004146:Dioxanes; D010447:Peptide Hydrolases
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