Crystallization and preliminary characterization of arabis mosaic virus.

ABSTRACT

Arabis mosaic virus, a member of the nepovirus group, was purified by a combination of differential centrifugation, gel filtration, and sucrose density gradient techniques. The molecular weight of the coat protein, estimated by SDS-polyacrylamide gel electrophoresis, and consideration of subunit packing indicated the surface lattice of the virion to be T = 1. The virus was stable to treatment with trypsin at neutral pH. The virus crystallizes in the cubic system, space group P2(1)3 with a = 387 A . There are four particles per unit cell, each situated on a crystallographic threefold axis.