Abstract
High resolution and high magnification electron micrographs of turnip yellow mosaic virus particles prepared by the negative staining procedure and the rotation technique are presented. Excellent agreement is found between these micrographs and a rhombic triacontahedron model with 32 subunits arranged in an icosahedral pattern with 5∶3∶2 symmetry. The protein shell of the virus is constructed of 32 morphological subunits. A discussion and interpretation of the electron microscope observations and the physico-chemical data is provided. All the evidence so far is strongly suggestive of 180 structural units representing possibly the total number of peptides in the virus protein shell. Some of the artifacts of the roration technique are also discussed.
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