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  • Title: Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex.
    Author: Debarnot C, Imbert I, Ferron F, Gluais L, Varlet I, Papageorgiou N, Bouvet M, Lescar J, Decroly E, Canard B.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2011 Mar 01; 67(Pt 3):404-8. PubMed ID: 21393853.
    Abstract:
    To date, the SARS coronavirus is the only known highly pathogenic human coronavirus. In 2003, it was responsible for a large outbreak associated with a 10% fatality rate. This positive RNA virus encodes a large replicase polyprotein made up of 16 gene products (nsp1-16), amongst which two methyltransferases, nsp14 and nsp16, are involved in viral mRNA cap formation. The crystal structure of nsp16 is unknown. Nsp16 is an RNA-cap AdoMet-dependent (nucleoside-2'-O-)-methyltransferase that is only active in the presence of nsp10. In this paper, the expression, purification and crystallization of nsp10 in complex with nsp16 are reported. The crystals diffracted to a resolution of 1.9 Å resolution and crystal structure determination is in progress.
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