Expression, purification, crystallization and preliminary crystallographic study of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1.
The voltage-gated proton channel Hv1 is essential to proton permeation and contains a voltage-sensor domain without a pore domain. It contains three predicted domains: an N-terminal acid and proline-rich domain, a transmembrane voltage-sensor domain and a C-terminal domain that is responsible for the dimeric architecture of Hv1. Here, the C-terminal domain of the human voltage-gated proton channel Hv1 (C-Hv1) was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals have a tetragonal form and diffraction data were collected to 2.5 A resolution in-house. The crystal belongs to space group P4(1)2(1)2, with unit-cell parameters a = b = 37.76, c = 137.52 A. Structural determination of C-Hv1 is in progress.
Li
Shu Jie
SJ
Department of Biophysics, Nankai University, Tianjin, People's Republic of China. shujieli@nankai.edu.cn
Zhao
Qing
Q
Zhou
Qiangjun
Q
Zhai
Yujia
Y
D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007473:Ion Channels / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D017434:Protein Structure, Tertiary
C510235:HVCN1 protein, human; D007473:Ion Channels