Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus
Author(s) -
Zhou Qingxian,
Rodgers John W.,
Barr John N.,
Green Todd J.,
Luo Ming
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106006397
Subject(s) - crystallization , virology , crystallography , protein crystallization , structural protein , virus , biology , chemistry , organic chemistry
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 C 2, 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.