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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1;63(Pt 5):426-9. Epub 2007 Apr 20.

Crystallization of the avian reovirus double-stranded RNA-binding and core protein sigmaA.

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1
Departamento de Bioquímica y Biología Molecular, Facultad de Farmacia, Universidad de Santiago de Compostela, Campus Sur, E-15782 Santiago de Compostela, Spain.

Abstract

The avian reovirus protein sigmaA plays a dual role: it is a structural protein forming part of the transcriptionally active core, but it has also been implicated in the resistance of the virus to interferon by strongly binding double-stranded RNA and thus inhibiting the double-stranded RNA-dependent protein kinase. The sigmaA protein has been crystallized from solutions containing ammonium sulfate at pH values around 6. Crystals belonging to space group P1, with unit-cell parameters a = 103.2, b = 129.9, c = 144.0 A, alpha = 93.8, beta = 105.1, gamma = 98.2 degrees were grown and a complete data set has been collected to 2.3 A resolution. The self-rotation function suggests that sigmaA may form symmetric arrangements in the crystals.

PMID:
17565188
PMCID:
PMC2335010
DOI:
10.1107/S1744309107017988
[Indexed for MEDLINE]
Free PMC Article
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