SrasV1, Main, Exploration, bibRecord, 002116

Expression, crystallization and preliminary crystallographic study of the C-terminal half of nsp2 from SARS coronavirus.

Identifieur interne : 002116 ( Main/Exploration ); précédent : 002115; suivant : 002117

Expression, crystallization and preliminary crystallographic study of the C-terminal half of nsp2 from SARS coronavirus.

Auteurs : Yuanyuan Li [République populaire de Chine] ; Zhilin Ren ; Zehua Bao ; Zhenhua Ming ; Xuemei Li

Source :

Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2011.

RBID : pubmed:21795795

Descripteurs français

English descriptors

KwdEn :
- Crystallization, Crystallography, X-Ray, Gene Expression, Models, Molecular, Protein Structure, Tertiary, SARS Virus (chemistry), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics).
MESH :
- chemical , chemistry : Viral Nonstructural Proteins.
- chemistry : SARS Virus.
- chemical , genetics : Viral Nonstructural Proteins.
- Crystallization, Crystallography, X-Ray, Gene Expression, Models, Molecular, Protein Structure, Tertiary.

Abstract

SARS coronavirus (SARS-CoV) is the aetiological agent of the highly infectious severe acute respiratory syndrome (SARS). To gain a better understanding of SARS-CoV replication and transcription proteins, a preliminary X-ray crystallographic study of the C-terminal domain of SARS-CoV nonstructural protein 2 (nsp2) is reported here. The C-terminal domain of SARS-CoV nsp2 was cloned, overexpressed, purified and crystallized using polyethylene glycol 5000 monomethyl ether as the precipitant; the crystals diffracted to 2.5 Å resolution. The crystals belonged to space group P6(5), with unit-cell parameters a=b=112.8, c=91.1 Å, α=β=90, γ=120°. One molecule is assumed to be present per asymmetric unit, which gives a Matthews coefficient of 2.89 Å3 Da(-1) and a solvent content of 56.2%.

DOI: 10.1107/S1744309111017829
PubMed: 21795795

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">SARS coronavirus (SARS-CoV) is the aetiological agent of the highly infectious severe acute respiratory syndrome (SARS). To gain a better understanding of SARS-CoV replication and transcription proteins, a preliminary X-ray crystallographic study of the C-terminal domain of SARS-CoV nonstructural protein 2 (nsp2) is reported here. The C-terminal domain of SARS-CoV nsp2 was cloned, overexpressed, purified and crystallized using polyethylene glycol 5000 monomethyl ether as the precipitant; the crystals diffracted to 2.5 Å resolution. The crystals belonged to space group P6(5), with unit-cell parameters a=b=112.8, c=91.1 Å, α=β=90, γ=120°. One molecule is assumed to be present per asymmetric unit, which gives a Matthews coefficient of 2.89 Å3 Da(-1) and a solvent content of 56.2%.</div>
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Expression, crystallization and preliminary crystallographic study of the C-terminal half of nsp2 from SARS coronavirus.

Expression, crystallization and preliminary crystallographic study of the C-terminal half of nsp2 from SARS coronavirus.

Source :

Descripteurs français

English descriptors

Abstract

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Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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