The atomic structure of the bluetongue virus core

Jonathan M. Grimes, J. Nicholas Burroughs, Patrice Gouet, Jonathan M. Diprose, Robyn Malby, Stephan Ziéntara, Peter P. C. Mertens and David I. Stuart ()
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Jonathan M. Grimes: The Laboratory of Molecular Biophysics, University of Oxford
J. Nicholas Burroughs: Institute of Animal Health, Pirbright Laboratory
Patrice Gouet: The Laboratory of Molecular Biophysics, University of Oxford
Jonathan M. Diprose: The Laboratory of Molecular Biophysics, University of Oxford
Robyn Malby: The Laboratory of Molecular Biophysics, University of Oxford
Stephan Ziéntara: C.N.E.V.A. Alfort, Laboratoire Central de Recherches Vétérinaires
Peter P. C. Mertens: Institute of Animal Health, Pirbright Laboratory
David I. Stuart: The Laboratory of Molecular Biophysics, University of Oxford

Nature, 1998, vol. 395, issue 6701, 470-478

Abstract: Abstract The structure of the core particle of bluetongue virus has been determined by X-ray crystallography at a resolution approaching 3.5 Å. This transcriptionally active compartment, 700 Å in diameter, represents the largest molecular structure determined in such detail. The atomic structure indicates how approximately 1,000 protein components self-assemble, using both the classical mechanism of quasi-equivalent contacts, which are achieved through triangulation, and a different method, which we term geometrical quasi-equivalence.

Date: 1998
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DOI: 10.1038/26694

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