Open AccessCrystallization and preliminary X‐ray diffraction studies of infectious bronchitis virus nonstructural protein 9
Author(s) -
Ma Yanlin,
Chen Cheng,
Wei Lei,
Yang Qingzhu,
Liao Ming,
Li Xuemei
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911001417x
Subject(s) - infectious bronchitis virus , virology , biology , rna , gene , escherichia coli , virus , capsid , transcription (linguistics) , crystallization , avian infectious bronchitis virus , genome , structural protein , coronavirus , microbiology and biotechnology , chemistry , covid-19 , genetics , infectious disease (medical specialty) , medicine , disease , linguistics , philosophy , organic chemistry , pathology
Avian infectious bronchitis virus (IBV), which causes respiratory disease in infected birds, belongs to coronavirus group 3. IBV encodes 15 nonstructural proteins (nsp2–nsp16) which play crucial roles in RNA transcription and genome replication. Nonstructural protein 9 (nsp9) has been identified as a protein that is essential to viral replication because of its single‐stranded RNA‐binding ability. The gene segment encoding IBV nsp9 has been cloned and expressed in Escherichia coli . The protein has been crystallized and the crystals diffracted X‐rays to 2.44 Å resolution. They belonged to the cubic space group I 432, with unit‐cell parameters a = b = c = 123.4 Å, α = β = γ = 90°. The asymmetric unit appeared to contain one molecule, with a solvent content of 62% ( V M = 3.26 Å 3 Da −1 ).