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VISP: Center for Viral Infection Structural Proteomics > VISPCollaboratorPublications > Purification, crystallization and preliminary X-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus  

VISPCollaboratorPublications: Purification, crystallization and preliminary X-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus

Title

Purification, crystallization and preliminary X-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus 

Authors

Rogers JW, et al. 

Abstract

Bunyamwera virus (BUNV) is the prototypic member of the Bunyaviridae family of segmented negative-sense RNA viruses. The BUNV nucleocapsid protein has been cloned and expressed in Escherichia coli. The purified protein has been crystallized and a complete data set has been collected to 3.3 angstroms resolution at a synchrotron source. Crystals of the nucleocapsid protein belong to space group C2, with unit-cell parameters a = 384.7, b = 89.8, c = 89.2 angstroms, beta = 94.4 degrees . Self-rotation function analysis of the X-ray diffraction data has provided insight into the oligomeric state of the protein as well as the orientation of the oligomers in the asymmetric unit. The structure determination of the protein is ongoing.

Journal

Acta Crystallograph Sect F Struct Biol Cryst Commun 

Date

1/4/2006 

Link

PMID: 16582485 

Reference

Rogers JW, Zhou Q, Green TJ, Barr JN, and Luo M. “Purification, crystallization and preliminary X-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus”. Acta Cryst. 2006 F62:361-364. (2006)

PMID

16582485 

Keyword

VISP, POX 
Attachments
Created at 3/1/2007 5:32 PM  by Sophie Coon 
Last modified at 3/1/2007 5:32 PM  by Sophie Coon