Open AccessCrystallization, high‐resolution data collection and preliminary crystallographic analysis of Aura virus capsid protease and its complex with dioxane
Author(s) -
Aggarwal Megha,
Dhindwal Sonali,
Pratap Shivendra,
Kuhn Richard J.,
Kumar Pravindra,
Tomar Shailly
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911103404x
Subject(s) - crystallization , capsid , crystallography , polyethylene glycol , resolution (logic) , protein crystallization , solvent , chemistry , protease , materials science , organic chemistry , biochemistry , enzyme , artificial intelligence , computer science , gene
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 C 2, 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%.