
Improved crystallization of the coxsackievirus B3 RNA‐dependent RNA polymerase
Author(s) -
Jabafi Ilham,
Selisko Barbara,
Coutard Bruno,
De Palma Armando M.,
Neyts Johan,
Egloff MariePierre,
Grisel Sacha,
Dalle Karen,
Campanacci Valerie,
Spinelli Silvia,
Cambillau Christian,
Canard Bruno,
Gruez Arnaud
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107020416
Subject(s) - coxsackievirus , picornaviridae , virology , enterovirus , poliovirus , rna , crystallization , myocarditis , serotype , virus , polymerase , rna polymerase , biology , dna , medicine , chemistry , gene , genetics , organic chemistry , cardiology
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 Å resolution and that were suitable for structure determination.