Open AccessPurification, crystallization and preliminary X‐ray analysis of nonstructural protein 2 (nsp2) from avian infectious bronchitis virus
Author(s) -
Yu Kun,
Ming Zhenhua,
Li Yuanyuan,
Chen Cheng,
Bao Zehua,
Ren Zhilin,
Liu Bofeng,
Tao Wei,
Rao Zihe,
Lou Zhiyong
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112018623
Subject(s) - avian infectious bronchitis virus , virology , recombinant dna , infectious bronchitis virus , biology , virus , escherichia coli , crystallization , spike protein , coronavirus , chemistry , covid-19 , genetics , medicine , gene , infectious disease (medical specialty) , disease , organic chemistry , pathology
Avian infectious bronchitis virus (IBV) is a member of the group III coronaviruses, which differ from the other groups of coronaviruses in that they do not encode the essential pathogenic factor nonstructural protein 1 (nsp1) and instead start with nsp2. IBV nsp2 is one of the first replicase proteins to be translated and processed in the viral life cycle; however, it has an entirely unknown function. In order to better understand the structural details and functional mechanism of IBV nsp2, the recombinant protein was cloned, overexpressed in Escherichia coli , purified and crystallized. The crystals diffracted to 2.8 Å resolution and belonged to space group P 2 1 , with unit‐cell parameters a = 57.0, b = 192.3, c = 105.7 Å, β = 90.8°. Two molecules were found in the asymmetric unit; the Matthews coefficient was 3.9 Å 3 Da −1 , corresponding to a solvent content of 68.2%.