Related Experiment Video
Updated: Jun 12, 2026
Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
Published on: June 28, 2013
Crystallization and preliminary X-ray diffraction studies of infectious bronchitis virus nonstructural protein 9
Yanlin Ma1, Cheng Chen, Lei Wei
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, People's Republic of China.
Abstract:
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 A resolution. They belonged to the cubic space group I432, with unit-cell parameters a = b = c = 123.4 A, alpha = beta = gamma = 90 degrees . The asymmetric unit appeared to contain one molecule, with a solvent content of 62% (V(M) = 3.26 A(3) Da(-1)).
