Crystallization, high-resolution data collection and preliminary crystallographic analysis of Aura virus capsid protease and its complex with dioxane.

Aggarwal M, Dhindwal S, Pratap S, Kuhn RJ, Kumar P, Tomar S.

Citation

Aggarwal M, Dhindwal S, Pratap S, Kuhn RJ, Kumar P, Tomar S. (2011) Crystallization, high-resolution data collection and preliminary crystallographic analysis of Aura virus capsid protease and its complex with dioxane. Acta Crystallographica. Sect F, Structural Biology and Crystallization Communications 67(Pt 11):1394-1398.

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 Ã?. High-resolution data sets were collected to a resolution of 1.81 Ã? for the native protein and 1.98 Ã? 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%.