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Rice dwarf virus (RDV) is a double-shelled icosahedral virus. Using electron cryomicro-scopy and computer reconstruction techniques, we have determined a 3.3 nm resolution three-dimensional (3D) structure of the inner shell capsid without the outer shell and viral RNA. The results show that the inner shell is a thin, densely packed, smooth structure, which provides a scaffold for the full virus. A total of 120 copies of the major inner shell capsid protein P3 forms 60 dimers arranged in a T=1 icosahedral lattice. A close examination on the subunit packing of the T=1 inner core P3 with that of the T=13/ outer shell P8 indicated that P8 trimers connect with P3 through completely non-equivalent, yet highly specific, intermolecular interactions.
Using electron cryomicro-scopy and computer reconstruction techniques, we have determined a 3.3 nm resolution three-dimensional (3D) structure of the inner shell capsid without the outer shell and viral RNA . The results show that the inner shell is a thin, densely packed, smooth structure, which provides a scaffold for the full virus. A total of 120 copies of the major inner shell capsid protein P3 forms 60 dimers arranged in a T = 1 icosahedral A close examination on the subunit packing of the T = 1 inner core P3 with that of the T = 13 / outer shell P8 indicates that P8 trimers connect with P3 through completely non-equivalent, yet highly specific, intermolecular interactions.