Improved crystallization of the coxsackievirus B3 RNA-dependent RNA polymerase

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt 6):495-8. doi: 10.1107/S1744309107020416. Epub 2007 May 12.

Abstract

The Picornaviridae virus family contains a large number of human pathogens such as poliovirus, hepatitis A virus and rhinoviruses. Amongst the viruses belonging to the genus Enterovirus, several serotypes of coxsackievirus coexist for which neither vaccine nor therapy is available. Coxsackievirus B3 is involved in the development of acute myocarditis and dilated cardiomyopathy and is thought to be an important cause of sudden death in young adults. Here, the first crystal of a coxsackievirus RNA-dependent RNA polymerase is reported. Standard crystallization methods yielded crystals that were poorly suited to X-ray diffraction studies, with one axis being completely disordered. Crystallization was improved by testing crystallization solutions from commercial screens as additives. This approach yielded crystals that diffracted to 2.1 A resolution and that were suitable for structure determination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Enterovirus B, Human / enzymology*
  • Enterovirus B, Human / genetics
  • Gene Expression Regulation, Bacterial / physiology
  • RNA-Dependent RNA Polymerase / biosynthesis
  • RNA-Dependent RNA Polymerase / chemistry*
  • RNA-Dependent RNA Polymerase / genetics
  • RNA-Dependent RNA Polymerase / isolation & purification

Substances

  • RNA-Dependent RNA Polymerase