Cloning, expression, purification and crystallization of the N-domain from the α2 subunit of the membrane-spanning Na,K-ATPase protein

被引：7

作者：

Haue, L ^{[1
]}

Pedersen, PA ^{[1
]}

Jorgensen, PL ^{[1
]}

Håkansson, KO ^{[1
]}

机构：

[1] Univ Copenhagen, August Krogh Inst, Biomembrane Ctr, DK-2100 Copenhagen OE, Denmark

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷

关键词：

D O I：

10.1107/S0907444903008795

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The nucleotide-binding domain of the Na,K-ATPase ion pump was expressed with a His tag in Escherichia coli and purified. The soluble 24 kDa derivative consists of 214 amino-acid residues and was crystallized in the presence of NiCl2. The crystals belong to space group F23, with unit-cell parameters a = b = c = 147.5 Angstrom, and diffract to 3.1 Angstrom. Complete data sets could be collected from native and thimerosal-treated crystals frozen in 50% sucrose. Five mercury positions were found and initial SIR phases calculated.

引用

页码：1259 / 1261

页数：3

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