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About:
Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein
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wasabi.inria.fr
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Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
title
Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein
Creator
Canard, Bruno
Cambillau, Christian
Egloff, Marie-Pierre
Longhi, Sonia
Rancurel, Corinne
Snijder, Eric
Tocque, Fabienne
Dobbe, Jessika
Campanacci, Vale
Durousseau, Ce
Ferron, Franc
Salomoni, Aurelia
source
Medline; PMC
abstract
The aetiologic agent of the recent epidemics of Severe Acute Respiratory Syndrome (SARS) is a positive‐stranded RNA virus (SARS‐CoV) belonging to the Coronaviridae family and its genome differs substantially from those of other known coronaviruses. SARS‐CoV is transmissible mainly by the respiratory route and to date there is no vaccine and no prophylactic or therapeutic treatments against this agent. A SARS‐CoV whole‐genome approach has been developed aimed at determining the crystal structure of all of its proteins or domains. These studies are expected to greatly facilitate drug design. The genomes of coronaviruses are between 27 and 31.5 kbp in length, the largest of the known RNA viruses, and encode 20–30 mature proteins. The functions of many of these polypeptides, including the Nsp9–Nsp10 replicase‐cleavage products, are still unknown. Here, the cloning, Escherichia coli expression, purification and crystallization of the SARS‐CoV Nsp9 protein, the first SARS‐CoV protein to be crystallized, are reported. Nsp9 crystals diffract to 2.8 Å resolution and belong to space group P6(1/5)22, with unit‐cell parameters a = b = 89.7, c = 136.7 Å. With two molecules in the asymmetric unit, the solvent content is 60% (V (M) = 3.1 Å(3) Da(−1)).
has issue date
2004-06-07
(
xsd:dateTime
)
bibo:doi
10.1107/s0907444903016779
bibo:pmid
12925794
has license
no-cc
sha1sum (hex)
afc29ba38f925a7d3ed22338b5a9b34f4b30a49c
schema:url
https://doi.org/10.1107/s0907444903016779
resource representing a document's title
Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein
has PubMed Central identifier
PMC7161644
has PubMed identifier
12925794
schema:publication
Acta Crystallogr D Biol Crystallogr
resource representing a document's body
covid:afc29ba38f925a7d3ed22338b5a9b34f4b30a49c#body_text
is
schema:about
of
named entity 'expected'
named entity 'positive-stranded'
named entity 'SARS-CoV'
named entity 'domains'
named entity 'Crystallography'
named entity 'protein'
named entity 'Severe Acute Respiratory Syndrome (SARS)'
named entity 'family'
named entity 'cloning'
named entity 'asymmetric unit'
named entity 'SARS-CoV'
named entity 'PROTEIN'
named entity 'lysozyme'
named entity 'sulfate'
named entity 'genomes'
named entity 'RNA virus'
named entity 'vaccine'
named entity 'viruses'
named entity 'genome'
named entity 'Escherichia coli'
named entity 'positive-stranded RNA virus'
named entity 'SARS-CoV'
named entity 'prophylactic'
named entity 'Coronaviridae'
named entity 'asymmetric unit'
named entity 'unit-cell parameters'
named entity 'protein'
named entity 'crystallization'
named entity 'genome'
named entity 'asymmetric unit'
named entity 'SARS'
named entity 'chaperones'
named entity 'E. coli'
named entity 'perinuclear region'
named entity 'SARS-CoV'
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named entity 'reverse transcriptase'
named entity 'subcloned'
named entity 'Ribavirin'
named entity 'cDNA'
named entity 'pandemic outbreaks'
named entity 'vaccine'
named entity 'epidemics'
named entity 'proteinase'
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named entity 'SARS-CoV'
named entity 'mouse hepatitis virus'
named entity 'antiviral drugs'
named entity 'drug design'
named entity 'pH 4'
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named entity 'ammonium sulfate'
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named entity 'NaCl'
named entity 'primers'
named entity 'SARS-CoV'
named entity 'Coronaviruses'
named entity 'quarantine'
named entity 'cloning'
named entity 'kbp'
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