Open AccessExpression, purification, crystallization and preliminary crystallographic study of the carboxyl‐terminal domain of the human voltage‐gated proton channel Hv1
Author(s) -
Li Shu Jie,
Zhao Qing,
Zhou Qiangjun,
Zhai Yujia
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109003777
Subject(s) - crystallization , tetragonal crystal system , crystallography , domain (mathematical analysis) , proton , resolution (logic) , chemistry , materials science , crystal structure , physics , mathematical analysis , mathematics , organic chemistry , quantum mechanics , artificial intelligence , computer science
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 Å resolution in‐house. The crystal belongs to space group P 4 1 2 1 2, with unit‐cell parameters a = b = 37.76, c = 137.52 Å. Structural determination of C‐Hv1 is in progress.