Cloning, expression, purification, crystallization and preliminary crystallographic study of the protein module (BIV2-Helix) in the fusion core of bovine immunodeficiency-like virus (BIV) gp40.
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 R3, with unit-cell parameters a = 39.17, b = 39.17, c = 295.05 A and two molecules per asymmetric unit. X-ray diffraction data were collected to 1.76 A in the home laboratory from a single crystal.
Zhao
Xiaodong
X
Laboratory of Structural Biology, Tsinghua University, Beijing 100084, People's Republic of China.
Li
Ming
M
Xu
Yanhui
Y
Lou
Zhiyong
Z
Meng
Zhaohui
Z
Li
Shu
S
Tian
Bo
B
Gao
George F
GF
Rao
Zihe
Z
D003001:Cloning, Molecular; D003460:Crystallization; D016087:Immunodeficiency Virus, Bovine / Q000235:genetics*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D014759:Viral Envelope Proteins