Open AccessCrystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex
Author(s) -
Debarnot Claire,
Imbert Isabelle,
Ferron François,
Gluais Laure,
Varlet Isabelle,
Papageorgiou Nicolas,
Bouvet Mickaël,
Lescar Julien,
Decroly Etienne,
Canard Bruno
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111002867
Subject(s) - coronavirus , rna , methyltransferase , resolution (logic) , crystallization , virology , messenger rna , biology , subgenomic mrna , crystallography , covid-19 , chemistry , gene , biochemistry , medicine , disease , organic chemistry , pathology , methylation , artificial intelligence , computer science , infectious disease (medical specialty)
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.