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Title: Preliminary crystallographic analysis of avian infectious bronchitis virus main protease

Abstract

The avian infectious bronchitis virus main protease has been crystallized; crystals diffract to 2.7 Å resolution. Infectious bronchitis virus (IBV) is the prototype of the genus Coronavirus. It causes a highly contagious disease which affects the respiratory, reproductive, neurological and renal systems of chickens, resulting great economic losses in the poultry industry worldwide. The coronavirus (CoV) main protease (M{sup pro}), which plays a pivotal role in viral gene expression and replication through a highly complex cascade involving the proteolytic processing of replicase polyproteins, is an attractive target for antiviral drug design. In this study, IBV M{sup pro} was overexpressed in Escherichia coli. Crystals suitable for X-ray crystallography have been obtained using microseeding techniques and belong to space group P6{sub 1}22. X-ray diffraction data were collected in-house to 2.7 Å resolution from a single crystal. The unit-cell parameters were a = b = 119.1, c = 270.7 Å, α = β = 90, γ = 120°. Three molecules were predicted to be present in the asymmetric unit from a calculated self-rotation function.

Authors:
;  [1];  [2];  [1];  [3]
  1. Laboratory of Structural Biology, Tsinghua University, Beijing 100084 (China)
  2. Laboratory of Avian Medicine, College of Veterinary Medicine, South China Agricultural University, Guangzhou 510642 (China)
  3. (China)
Publication Date:
OSTI Identifier:
22360254
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 1; Other Information: PMCID: PMC2330114; PMID: 17183167; PUBLISHER-ID: pu5171; OAI: oai:pubmedcentral.nih.gov:2330114; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLOGRAPHY; DESIGN; ESCHERICHIA COLI; LOSSES; MOLECULES; MONOCRYSTALS; PROCESSING; RESOLUTION; ROTATION; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats

Li, Jun, Shen, Wei, Liao, Ming, E-mail: mliao@scau.edu.cn, Bartlam, Mark, E-mail: mliao@scau.edu.cn, and National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101. Preliminary crystallographic analysis of avian infectious bronchitis virus main protease. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309106052341.
Li, Jun, Shen, Wei, Liao, Ming, E-mail: mliao@scau.edu.cn, Bartlam, Mark, E-mail: mliao@scau.edu.cn, & National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101. Preliminary crystallographic analysis of avian infectious bronchitis virus main protease. United Kingdom. doi:10.1107/S1744309106052341.
Li, Jun, Shen, Wei, Liao, Ming, E-mail: mliao@scau.edu.cn, Bartlam, Mark, E-mail: mliao@scau.edu.cn, and National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101. Mon . "Preliminary crystallographic analysis of avian infectious bronchitis virus main protease". United Kingdom. doi:10.1107/S1744309106052341.
@article{osti_22360254,
title = {Preliminary crystallographic analysis of avian infectious bronchitis virus main protease},
author = {Li, Jun and Shen, Wei and Liao, Ming, E-mail: mliao@scau.edu.cn and Bartlam, Mark, E-mail: mliao@scau.edu.cn and National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101},
abstractNote = {The avian infectious bronchitis virus main protease has been crystallized; crystals diffract to 2.7 Å resolution. Infectious bronchitis virus (IBV) is the prototype of the genus Coronavirus. It causes a highly contagious disease which affects the respiratory, reproductive, neurological and renal systems of chickens, resulting great economic losses in the poultry industry worldwide. The coronavirus (CoV) main protease (M{sup pro}), which plays a pivotal role in viral gene expression and replication through a highly complex cascade involving the proteolytic processing of replicase polyproteins, is an attractive target for antiviral drug design. In this study, IBV M{sup pro} was overexpressed in Escherichia coli. Crystals suitable for X-ray crystallography have been obtained using microseeding techniques and belong to space group P6{sub 1}22. X-ray diffraction data were collected in-house to 2.7 Å resolution from a single crystal. The unit-cell parameters were a = b = 119.1, c = 270.7 Å, α = β = 90, γ = 120°. Three molecules were predicted to be present in the asymmetric unit from a calculated self-rotation function.},
doi = {10.1107/S1744309106052341},
journal = {Acta Crystallographica. Section F},
number = Pt 1,
volume = 63,
place = {United Kingdom},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}