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Title: Crystallization of the avian reovirus double-stranded RNA-binding and core protein σA

Abstract

The avian reovirus double-stranded RNA-binding and core protein σA has been crystallized in 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°. A complete data set has been collected to 2.3 Å resolution and analyzed. 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.

Authors:
;  [1];  [2];  [3]; ; ;  [1];  [1];  [4]
  1. Departamento de Bioquímica y Biología Molecular, Facultad de Farmacia, Universidad de Santiago de Compostela, Campus Sur, E-15782 Santiago de Compostela (Spain)
  2. Unidad 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)
  3. Spanish CRG Beamline BM16, European Synchrotron Radiation Facility (ESRF), 6 Rue Jules Horowitz, BP 220, F-38043 Grenoble (France)
  4. (Spain)
Publication Date:
OSTI Identifier:
22363935
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2335010; PMID: 17565188; PUBLISHER-ID: ll5111; OAI: oai:pubmedcentral.nih.gov:2335010; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AMMONIUM SULFATES; CRYSTALLIZATION; CRYSTALS; MATHEMATICAL SOLUTIONS; PH VALUE; RESOLUTION; ROTATION; SOLUTIONS; SPACE GROUPS

Citation Formats

Hermo-Parrado, X. Lois, Guardado-Calvo, Pablo, Llamas-Saiz, Antonio L., Fox, Gavin C., Vazquez-Iglesias, Lorena, Martínez-Costas, José, Benavente, Javier, Raaij, Mark J. van, E-mail: vanraaij@usc.es, and Unidad 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. Crystallization of the avian reovirus double-stranded RNA-binding and core protein σA. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107017988.
Hermo-Parrado, X. Lois, Guardado-Calvo, Pablo, Llamas-Saiz, Antonio L., Fox, Gavin C., Vazquez-Iglesias, Lorena, Martínez-Costas, José, Benavente, Javier, Raaij, Mark J. van, E-mail: vanraaij@usc.es, & Unidad 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. Crystallization of the avian reovirus double-stranded RNA-binding and core protein σA. United Kingdom. doi:10.1107/S1744309107017988.
Hermo-Parrado, X. Lois, Guardado-Calvo, Pablo, Llamas-Saiz, Antonio L., Fox, Gavin C., Vazquez-Iglesias, Lorena, Martínez-Costas, José, Benavente, Javier, Raaij, Mark J. van, E-mail: vanraaij@usc.es, and Unidad 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. Tue . "Crystallization of the avian reovirus double-stranded RNA-binding and core protein σA". United Kingdom. doi:10.1107/S1744309107017988.
@article{osti_22363935,
title = {Crystallization of the avian reovirus double-stranded RNA-binding and core protein σA},
author = {Hermo-Parrado, X. Lois and Guardado-Calvo, Pablo and Llamas-Saiz, Antonio L. and Fox, Gavin C. and Vazquez-Iglesias, Lorena and Martínez-Costas, José and Benavente, Javier and Raaij, Mark J. van, E-mail: vanraaij@usc.es and Unidad 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},
abstractNote = {The avian reovirus double-stranded RNA-binding and core protein σA has been crystallized in 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°. A complete data set has been collected to 2.3 Å resolution and analyzed. 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.},
doi = {10.1107/S1744309107017988},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}