The structure of the core particle of bluetongue virus has been determ
ined by X-ray crystallography at a resolution approaching 3.5 Angstrom
. This transcriptionally active compartment, 700 Angstrom in diameter,
represents the largest molecular structure determined in such detail.
The atomic structure Indicates how approximately 1,000 protein compon
ents self-assemble, using both the classical mechanism of quasi-equiva
lent contacts, which are achieved through triangulation, and a differe
nt method, which we term geometrical quasi-equivalence.