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Abstract:
Tobacco mosaic virus coat protein has been repolymerized in the absence of RNA and investigated by X-ray analysis. The rods obtained can be classified in two different helical surface lattices (class A and B), having nearly 16 1/3 and 17 1/3 subunits per turn, respectively, with only small differences in polypeptide chain folding. The structure of the protein rod in helix class A is almost identical with that in intact tobacco mosaic virus, while in the absence of the RNA the class B surface lattice is predominant.