title: Crystallization of the avian reovirus double-stranded RNA-binding and core protein sigmaA.
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.
authors.affiliation: Departamento de Bioquímica y Biología Molecular, Facultad de Farmacia, Universidad de Santiago de Compostela, Campus Sur, E-15782 Santiago de Compostela, Spain.
authors.forename: X Lois
authors.initials: XL
authors.lastname: Hermo-Parrado
authors.forename: Pablo
authors.initials: P
authors.lastname: Guardado-Calvo
authors.forename: Antonio L
authors.initials: AL
authors.lastname: Llamas-Saiz
authors.forename: Gavin C
authors.initials: GC
authors.lastname: Fox
authors.forename: Lorena
authors.initials: L
authors.lastname: Vazquez-Iglesias
authors.forename: José
authors.initials: J
authors.lastname: Martínez-Costas
authors.forename: Javier
authors.initials: J
authors.lastname: Benavente
authors.forename: Mark J
authors.initials: MJ
authors.lastname: van Raaij
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D030101:Orthoreovirus, Avian / Q000737:chemistry*; D011487:Protein Conformation; D016601:RNA-Binding Proteins / Q000737:chemistry*; D014758:Viral Core Proteins / Q000737:chemistry*
chemical_list: D016601:RNA-Binding Proteins; D014758:Viral Core Proteins; C403292:sigmaA protein, avian reovirus