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.
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Acknowledgements
We thank the SRS, ESRF and EMBL for their assistance in data collection, in particular the staff of ID2 at the ESRF; the disease security officers D. Goodridge, S. Williams, A. Meyer and P. Wilkinson; M. Pickford for technical assistance; R. Bryan, K. Measures and R. Esnouf for computing; S. Lee for assistance with figures; and P. Roy and E. Y. Jones for discussion. This work has been given long-term support by the BBSRC and MRC; R.M. is supported by a C. J. Martin fellowship from NHMRC Australia; P.P.C.M. and J.N.B. are supported by MAFF.
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Grimes, J., Burroughs, J., Gouet, P. et al. The atomic structure of the bluetongue virus core. Nature 395, 470–478 (1998). https://doi.org/10.1038/26694
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DOI: https://doi.org/10.1038/26694
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