Functional implications of quasi-equivalence in a T=3 icosahedral animal virus established by cryo-electron microscopy and X-ray crystallography
- 1 April 1994
- Vol. 2 (4) , 271-282
- https://doi.org/10.1016/s0969-2126(00)00029-0
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstructionThe Journal of cell biology, 1993
- Ordered duplex RNA controls capsid architecture in an icosahedral animal virusNature, 1993
- Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallographyNature, 1992
- Three-dimensional structure of myosin subfragment-1 from electron microscopy of sectioned crystals.The Journal of cell biology, 1991
- Extension of molecular replacement: a new search strategy based on Patterson correlation refinementActa Crystallographica Section A Foundations of Crystallography, 1990
- The T=4 envelope of sindbis virus is organized by interactions with a complementary T=3 capsidCell, 1987
- Evidence for a Divided Genome in Nodamura Virus, an Arthropod-borne PicornavirusJournal of General Virology, 1973
- The Structure of Heated Poliovirus ParticlesJournal of General Virology, 1971
- Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographsPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1971
- Physical Principles in the Construction of Regular VirusesCold Spring Harbor Symposia on Quantitative Biology, 1962