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The structure of the core particle of bluetongue virus has been determined by X-ray crystallography at a resolution approaching 3.5 A. This transcriptionally active compartment, 700 A 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.

Original publication

DOI

10.1038/26694

Type

Journal article

Journal

Nature

Publication Date

01/10/1998

Volume

395

Pages

470 - 478

Keywords

Amino Acid Sequence, Bluetongue virus, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, RNA, Viral, Viral Core Proteins