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Acta Crystallogr Sect F Struct Biol Cryst Commun. May 1, 2007; 63(Pt 5): 426–429.
Published online Apr 20, 2007. doi:  10.1107/S1744309107017988
PMCID: PMC2335010
Crystallization of the avian reovirus double-stranded RNA-binding and core protein σA
X. Lois Hermo-Parrado,a Pablo Guardado-Calvo,a Antonio L. Llamas-Saiz,b Gavin C. Fox,c Lorena Vazquez-Iglesias,a José Martínez-Costas,a Javier Benavente,a and Mark J. van Raaijab*
aDepartamento de Bioquímica y Biología Molecular, Facultad de Farmacia, Universidad de Santiago de Compostela, Campus Sur, E-15782 Santiago de Compostela, Spain
bUnidad de Difracción de Rayos X, Laboratorio Integral de Dinámica y Estructura de Biomoléculas José R. Carracido, Edificio CACTUS, Universidad de Santiago de Compostela, Campus Sur, E-15782 Santiago de Compostela, Spain
cSpanish CRG Beamline BM16, European Synchrotron Radiation Facility (ESRF), 6 Rue Jules Horowitz, BP 220, F-38043 Grenoble, France
Correspondence e-mail: vanraaij/at/usc.es
Received March 16, 2007; Accepted April 10, 2007.
Abstract
The avian reovirus protein σA 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 σA 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 Å, α = 93.8, β = 105.1, γ = 98.2° were grown and a complete data set has been collected to 2.3 Å resolution. The self-rotation function suggests that σA may form symmetric arrangements in the crystals.
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International Union of Crystallography