Electron cryo-microscopy and image reconstruction of adeno-associated virus type 2 empty capsids

Adeno-associated virus type 2 empty capsids are composed of three proteins, VP1, VP2 and VP3, which have relative molecular masses of 87, 72 and 62 kD a, respectively, and differ in their N-terminal amino acid sequences. They have a likely molar ratio of 1:1:8 and occupy symmetrical equivalent positi ons in an icosahedrally arranged protein shell. We have investigated empty capsids of adeno-associated virus type 2 by electron cryo-microscopy and ic osahedral image reconstruction. The three-dimensional map at 1.05 nm resolu tion showed sets of three elongated spikes surrounding the three-fold symme try axes and narrow empty channels at the five-fold axes. The inside of the capsid superimposed with the previously determined structure of the canine parvovirus (Q. Me and M.S. Chapman, 1996, J. Mol. BioL, 264, 497-520), whe reas the outer surface showed clear discrepancies. Globular structures at t he inner surface of the capsid at the two-fold symmetry axes were identifie d as possible positions for the N-terminal extensions of VP1 and VP2.