Key result
Using crystallization solutions from commercial screens as additives improved the crystallization of coxsackievirus B3 RNA-dependent RNA polymerase, yielding crystals that diffracted to 2.1 A resolution.
Improved crystallization methods yielded high-resolution crystals of the coxsackievirus B3 RNA-dependent RNA polymerase, enabling future structural studies for a virus implicated in acute myocarditis and dilated cardiomyopathy.
May aid structural studies of viral RdRPs; leaves open generalizability of commercial screen additives.
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.
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Jabafi et al. (2007) studied Coxsackievirus B3. Crystallization solutions from commercial screens as additives vs. Standard crystallization methods was evaluated on Crystal diffraction resolution. Using crystallization solutions from commercial screens as additives improved the crystallization of coxsackievirus B3 RNA-dependent RNA polymerase, yielding crystals that diffracted to 2.1 A resolution.
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