Abstract
Reassembled alfalfa mosaic virus coat protein was partially digested with trypsin to remove the first 26 amino acids (Bol et al., 1974). These particles are empty icosahedral protein shells built with 60 alfalfa mosaic virus protein subunits. This aggregate has been crystallized in two different crystal forms, one of which diffracts X-rays to at least 3.4 Å resolution. The type I crystals (space group P6 3, a = 200 A ̊ , c = 314 A ̊ ) contain two particles per cell separated by 195 Å with each sitting on a 3-fold axis. The type II crystals contain three particles per cell in space group P3 1or P3 2 ( a = 201 A ̊ , c = 485 A ̊ ). Other T = 1 viral particles have very similar diameters.
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