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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt 4):361-4. doi: 10.1107/S1744309106006397. Epub 2006 Mar 10.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bunyamwera virus / chemistry*
  • Crystallography, X-Ray
  • Macromolecular Substances
  • Nucleocapsid Proteins / chemistry*
  • Nucleocapsid Proteins / isolation & purification
  • Viral Proteins / chemistry
  • Viral Proteins / isolation & purification
  • X-Ray Diffraction

Substances

  • Macromolecular Substances
  • Nucleocapsid Proteins
  • Viral Proteins