Open AccessCrystallization of the avian reovirus double‐stranded RNA‐binding and core protein σA
Author(s) -
HermoParrado X. Lois,
GuardadoCalvo Pablo,
LlamasSaiz Antonio L.,
Fox Gavin C.,
VazquezIglesias Lorena,
MartínezCostas José,
Benavente Javier,
Van Raaij Mark J.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107017988
Subject(s) - rna , crystallization , chemistry , capsid , ammonium sulfate , crystallography , microbiology and biotechnology , biology , biochemistry , gene , organic chemistry , chromatography
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 P 1, 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.