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
收藏
页码：1259 / 1261
页数：3
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