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Journal Articles Acta crystallographica Section F : Structural biology communications [2014-...] Year : 2011

Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex.

Isabelle Imbert
Francois Ferron
Laure Gluais
  • Function : Author
Nicolas Papageorgiou
  • Function : Author
Mickaël Bouvet
  • Function : Author
  • PersonId : 767256
  • IdRef : 090490169
Julien Lescar
Bruno Canard

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.

Dates and versions

hal-00751530 , version 1 (13-11-2012)

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Cite

Claire Debarnot, Isabelle Imbert, Francois Ferron, Laure Gluais, Isabelle Varlet, et al.. Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex.. Acta crystallographica Section F : Structural biology communications [2014-..], 2011, 67 (Pt 3), pp.404-8. ⟨10.1107/S1744309111002867⟩. ⟨hal-00751530⟩
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