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

Abstract

The nucleocapsid protein of Bunyamwera virus, the prototypic member of the Bunyaviridae family of segmented negative-sense RNA viruses, has been expressed and crystallized. Complete X-ray diffraction data sets have been collected. 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 Å 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 Å, β = 94.4°. 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.

Authors:
; ; ; ;  [1]
  1. Department of Microbiology, School of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294 (United States)
Publication Date:
OSTI Identifier:
22356345
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 4; Other Information: PMCID: PMC2222577; PMID: 16582485; PUBLISHER-ID: pu5130; OAI: oai:pubmedcentral.nih.gov:2222577; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; ESCHERICHIA COLI; ORIENTATION; PROTEINS; RESOLUTION; ROTATION; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats

Rodgers, John W., Zhou, Qingxian, Green, Todd J., Barr, John N., and Luo, Ming, E-mail: mingluo@uab.edu. Purification, crystallization and preliminary X-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106006397.
Rodgers, John W., Zhou, Qingxian, Green, Todd J., Barr, John N., & Luo, Ming, E-mail: mingluo@uab.edu. Purification, crystallization and preliminary X-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus. United Kingdom. doi:10.1107/S1744309106006397.
Rodgers, John W., Zhou, Qingxian, Green, Todd J., Barr, John N., and Luo, Ming, E-mail: mingluo@uab.edu. Sat . "Purification, crystallization and preliminary X-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus". United Kingdom. doi:10.1107/S1744309106006397.
@article{osti_22356345,
title = {Purification, crystallization and preliminary X-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus},
author = {Rodgers, John W. and Zhou, Qingxian and Green, Todd J. and Barr, John N. and Luo, Ming, E-mail: mingluo@uab.edu},
abstractNote = {The nucleocapsid protein of Bunyamwera virus, the prototypic member of the Bunyaviridae family of segmented negative-sense RNA viruses, has been expressed and crystallized. Complete X-ray diffraction data sets have been collected. 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 Å 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 Å, β = 94.4°. 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.},
doi = {10.1107/S1744309106006397},
journal = {Acta Crystallographica. Section F},
number = Pt 4,
volume = 62,
place = {United Kingdom},
year = {Sat Apr 01 00:00:00 EST 2006},
month = {Sat Apr 01 00:00:00 EST 2006}
}