Reference:
Cheng, R. H., V. Reddy, N. H. Olson, A. Fisher, T. S. Baker, and J. E. Johnson
(1994) Functional implications of quasi-equivalence in a T=3 icosahedral animal
virus established by cryo-electron microscopy and x-ray crystallography.
Structure 2:271-282.
This is the structure of Flock House Virus (FHV) solved by a combination of cryo-electron microscopy and X-ray crystallography. The FHV model in the center is superimposed over the two types of raw data used to compute the model: a transmission electron micrograph of virus particles (green region) and an X-ray diffraction pattern of a virus crystal (bright spots against a brown background). The protein shell of FHV (blue) is computationally trimmed away to visualize the internal components including the viral RNA (red) and several a -helical g-peptides (cyan, red and green cylinders) which lie just inside the protein shell. These peptides interact wit h the viral RNA and act to control capsid assembly and viral uncoating.