SrasV1, PubMed, Checkpoint, bibRecord, 002238

Crystallization and preliminary X-ray diffraction analysis of Nsp15 from SARS coronavirus.

Identifieur interne : 002238 ( PubMed/Checkpoint ); précédent : 002237; suivant : 002239

Crystallization and preliminary X-ray diffraction analysis of Nsp15 from SARS coronavirus.

Auteurs : Stéfano Ricagno [France] ; Bruno Coutard ; Sacha Grisel ; Nicolas Brémond ; Karen Dalle ; Fabienne Tocque ; Valérie Campanacci ; Julie Lichière ; Violaine Lantez ; Claire Debarnot ; Christian Cambillau ; Bruno Canard ; Marie Pierre Egloff

Source :

Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2006.

RBID : pubmed:16582498

Descripteurs français

English descriptors

KwdEn :
- Cloning, Molecular, Crystallization, Escherichia coli, Macromolecular Substances (chemistry), Macromolecular Substances (isolation & purification), Peptide Fragments (chemistry), Protein Conformation, RNA Replicase (chemistry), RNA Replicase (genetics), RNA Replicase (isolation & purification), Recombinant Proteins (chemistry), Recombinant Proteins (isolation & purification), SARS Virus (chemistry), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (isolation & purification), X-Ray Diffraction.
MESH :
- chemical , chemistry : Macromolecular Substances, Peptide Fragments, RNA Replicase, Recombinant Proteins, Viral Nonstructural Proteins.
- chemical , genetics : RNA Replicase, Viral Nonstructural Proteins.
- chemical , isolation & purification : Macromolecular Substances, RNA Replicase, Recombinant Proteins, Viral Nonstructural Proteins.
- chemistry : SARS Virus.
- Cloning, Molecular, Crystallization, Escherichia coli, Protein Conformation, X-Ray Diffraction.

Abstract

The non-structural protein Nsp15 from the aetiological agent of SARS (severe acute respiratory syndrome) has recently been characterized as a uridine-specific endoribonuclease. This enzyme plays an essential role in viral replication and transcription since a mutation in the related H229E human coronavirus nsp15 gene can abolish viral RNA synthesis. SARS full-length Nsp15 (346 amino acids) has been cloned and expressed in Escherichia coli with an N-terminal hexahistidine tag and has been purified to homogeneity. The protein was subsequently crystallized using PEG 8000 or 10 000 as precipitants. Small cubic crystals of the apoenzyme were obtained from 100 nl nanodrops. They belong to space group P4(1)32 or P4(3)32, with unit-cell parameters a = b = c = 166.8 angstroms. Diffraction data were collected to a maximum resolution of 2.7 angstroms.

DOI: 10.1107/S1744309106009407
PubMed: 16582498

Affiliations:

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to stream PubMed, to step Corpus: 002290
to stream PubMed, to step Curation: 002290

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pubmed:16582498

Le document en format XML

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<front><div type="abstract" xml:lang="en">The non-structural protein Nsp15 from the aetiological agent of SARS (severe acute respiratory syndrome) has recently been characterized as a uridine-specific endoribonuclease. This enzyme plays an essential role in viral replication and transcription since a mutation in the related H229E human coronavirus nsp15 gene can abolish viral RNA synthesis. SARS full-length Nsp15 (346 amino acids) has been cloned and expressed in Escherichia coli with an N-terminal hexahistidine tag and has been purified to homogeneity. The protein was subsequently crystallized using PEG 8000 or 10 000 as precipitants. Small cubic crystals of the apoenzyme were obtained from 100 nl nanodrops. They belong to space group P4(1)32 or P4(3)32, with unit-cell parameters a = b = c = 166.8 angstroms. Diffraction data were collected to a maximum resolution of 2.7 angstroms.</div>
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Crystallization and preliminary X-ray diffraction analysis of Nsp15 from SARS coronavirus.

Crystallization and preliminary X-ray diffraction analysis of Nsp15 from SARS coronavirus.

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