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Crystallization of alfalfa mosaic virus coat protein as a T = 1 aggregate

1981; Elsevier BV; Volume: 150; Issue: 1 Linguagem: Inglês

10.1016/0022-2836(81)90323-5

1089-8638

Keiichi Fukuyama, Sherin S. Abdel‐Meguid, Michael G. Rossmann,

Plant and Fungal Interactions Research

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 P63, a = 200 Å, c = 314 Å) 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 P31or P32 (a = 201 Å, c = 485 Å). Other T = 1 viral particles have very similar diameters.