Expression, purification, crystallization and preliminary crystallographic study of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1

AUTHORS

Li SJShu Jie , Zhao QQing , Zhou QQiangjun , Zhai YYujia . Acta crystallographica. Section F, Structural biology and crystallization communications. 2009 2 26; 65(Pt 3). 279-81

PMID: 19255483[PubMed].
PMCID: PMC2650464.

ABSTRACT

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.

Tags: 2009