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.