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© Research
Publication : Acta crystallographica. Section F, Structural biology and crystallization communications

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 01 May 2007

Hermo-Parrado XL, Guardado-Calvo P, Llamas-Saiz AL, Fox GC, Vazquez-Iglesias L, Martínez-Costas J, Benavente J, van Raaij MJ,

Link to Pubmed [PMID] – 17565188

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

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.

https://pubmed.ncbi.nlm.nih.gov/17565188