ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Expression, crystallization and preliminary crystallographic study of mouse hepatitis virus (MHV) nucleocapsid protein C-terminal domain.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Mouse hepatitis virus (MHV) belongs to the group II coronaviruses. The virus produces nine genes encoding 11 proteins that could be recognized as structural proteins and nonstructural proteins and are crucial for viral RNA synthesis. The nucleocapsid (N) protein, one of the structural proteins, interacts with the 30.4 kb virus genomic RNA to form the helical nucleocapsid and associates with the membrane glycoprotein via its C-terminus to stabilize virion assembly. Here, the expression and crystallization of the MHV nucleocapsid protein C-terminal domain are reported. The crystals diffracted to 2.20 A resolution and belonged to space group P422, with unit-cell parameters a = 66.6, c = 50.8 A. Assuming the presence of two molecules in the asymmetric unit, the solvent content is 43.0% (V(M) = 2.16 A(3) Da(-1)).
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