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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1394-8. doi: 10.1107/S174430911103404X. Epub 2011 Oct 27.


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%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alphavirus / enzymology*
  • Capsid / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Dioxanes / chemistry*
  • Dioxanes / metabolism
  • Peptide Hydrolases / chemistry*


  • Dioxanes
  • Peptide Hydrolases