The determination of the structure of the transcriptionally active core par
ticle of bluetongue virus is discussed. This particle is approximately 700
Angstrom in diameter and reasonably well ordered, but fragile, crystals hav
e been obtained from two different serotypes of the virus. Cryocrystallogra
phy proved difficult and a large number of crystals were analysed at room t
emperature to accumulate a reasonably complete data set. The effects of syn
chrotron optics, station design and detector on the signal-to-noise for the
se weak data are discussed, with particular reference to station ID2 at the
European Synchrotron Radiation Facility. Once the data had been gathered,
structure determination was straightforward, using a model derived from a c
ombination of electron microscopy and protein crystallography to obtain ini
tial phases. Despite apparent isomorphism, it is suspected that the crystal
lattice 'ages', perhaps reflecting both the inevitable weakness of the for
ces holding crystals of such a large macromolecular complex together and fl
exibility in the particle.