About: Crystallization and diffraction analysis of the SARS coronavirus nsp10

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About: Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex
Creator	Canard, Bruno Decroly, Etienne Ferron, François Lescar, Julien Debarnot, Claire Gluais, Laure Imbert, Isabelle Papageorgiou, Nicolas Bouvet, Mickaël Varlet, Isabelle
source	Medline; PMC
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.
has issue date	2011-02-25(xsd:dateTime)
bibo:doi	10.1107/s1744309111002867
bibo:pmid	21393853
has license	bronze-oa
sha1sum (hex)	10c9cdfc6c7d6b87be6ecfacbcbf1e150d5b6906
schema:url	https://doi.org/10.1107/s1744309111002867
resource representing a document's title	Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex
has PubMed Central identifier	PMC3053173
has PubMed identifier	21393853
schema:publication	Acta Crystallographica Section F Structural Biology and Crystallization Communications
resource representing a document's body	covid:10c9cdfc6c7d6b87be6ecfacbcbf1e150d5b6906#body_text
is schema:about of	named entity 'STRUCTURAL BIOLOGY' named entity 'highly' named entity 'crystal structure' named entity 'complex' named entity 'Crystallization' named entity 'COMPLEX' named entity 'METHYLTRANSFERASES' named entity 'SARS CORONAVIRUS' named entity 'CRYSTAL STRUCTURE' named entity 'EXPRESSION' named entity 'DATE' named entity 'POLYPROTEIN' named entity 'CRYSTALS' named entity 'COMPLEX' named entity 'CRYSTALLIZATION' named entity 'PURIFICATION' named entity 'PRESENCE OF' named entity 'GENE' named entity 'UNKNOWN' named entity 'CAP' named entity 'KNOWN' named entity 'VIRAL MRNA' named entity 'CRYSTALLIZATION' named entity 'DIFFRACTION ANALYSIS' named entity 'PRODUCTS' named entity 'POSITIVE' named entity 'DEPENDENT' named entity 'COMMUNICATIONS' named entity 'ADOMET' named entity 'RATE' named entity 'HIGHLY' named entity 'OUTBREAK' named entity 'SARS CORONAVIRUS' named entity 'ASSOCIATED WITH' named entity 'RESPONSIBLE' named entity '1.9' named entity 'STRUCTURE DETERMINATION' named entity 'INVOLVED' named entity 'REPORTED' named entity '10%' named entity 'RNA' named entity 'ACTIVE' named entity 'RESOLUTION' named entity 'LARGE' named entity 'IN PROGRESS' named entity 'REPLICASE' named entity 'HUMAN CORONAVIRUS' named entity 'METHYLTRANSFERASE' named entity 'FORMATION' named entity 'PAPER' named entity 'RNA VIRUS' named entity 'PATHOGENIC' named entity 'positive' named entity 'mRNA' named entity 'RNA virus' named entity 'diffracted' named entity 'resolution' named entity 'nucleoside' named entity 'methyltransferase' named entity 'cap formation' named entity 'crystal structure' named entity 'Structural Biology' named entity '1, 2' named entity 'mRNA capping' named entity 'SDS-PAGE' named entity 'nucleotide' named entity 'diffusion' named entity 'space group' named entity 'methyltransferase' named entity 'amino acids' named entity 'van Vliet' named entity 'bicine'

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