Purification, crystallization and X-ray diffraction analysis of the C-terminal protease domain of Venezuelan equine encephalitis virus nsP2

Andrew T. Russo, Stanley Watowich

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The C-terminal region of Venezuelan equine encephalitis virus (VEEV) nsP2 is responsible for proteolytic processing of the VEEV polyprotein replication complex. This action regulates the activity of the replication complex and is essential for viral replication, thus making nsP2 a very attractive target for development of VEEV therapeutics. The 338-amino-acid C-terminal region of VEEV nsP2 has been overexpressed in Escherichia coli, purified and crystallized. Crystals diffract to beyond 2.5 Å resolution and belong to the orthorhombic space group P212121. Isomorphous heavy-atom derivatives suitable for phase analysis have been obtained and work on building a complete structural model is under way.

Original languageEnglish (US)
Pages (from-to)514-517
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number6
DOIs
StatePublished - Jun 2006

Fingerprint

encephalitis
Venezuelan Equine Encephalitis Viruses
protease
viruses
Crystallization
Viruses
purification
X-Ray Diffraction
X ray diffraction analysis
Purification
Peptide Hydrolases
crystallization
diffraction
x rays
Polyproteins
Structural Models
Virus Replication
Escherichia
Escherichia coli
amino acids

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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