Open AccessCloning, expression, purification, crystallization and preliminary crystallographic study of the protein module (BIV2‐Helix) in the fusion core of bovine immunodeficiency‐like virus (BIV) gp40
Author(s) -
Zhao Xiaodong,
Li Ming,
Xu Yanhui,
Lou Zhiyong,
Meng Zhaohui,
Li Shu,
Tian Bo,
Gao George F.,
Rao Zihe
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105002174
Subject(s) - crystallization , crystallography , cloning (programming) , recombinant dna , escherichia coli , fusion protein , helix (gastropod) , virology , core (optical fiber) , biology , crystal (programming language) , microbiology and biotechnology , materials science , chemistry , biochemistry , gene , ecology , organic chemistry , snail , computer science , composite material , programming language
The fusion core of bovine immunodeficiency virus (BIV) gp40 is proposed to be involved in membrane fusion. However, no crystal structures are yet available. A predicted protein module BIV2‐Helix of BIVgp40 has been expressed in Escherichia coli and purified by chromatography. Recombinant BIV2‐Helix was crystallized using the hanging‐drop vapour‐diffusion technique at 291 K. The crystals were grown in MPD and belonged to the primitive rhombohedral space group R 3, with unit‐cell parameters a = 39.17, b = 39.17, c = 295.05 Å and two molecules per asymmetric unit. X‐ray diffraction data were collected to 1.76 Å in the home laboratory from a single crystal.