Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein

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 NiCl(2). The crystals belong to space group F23, with unit-cell parameter...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-07, Vol.59 (Pt 7), p.1259-1261
Hauptverfasser:	Haue, Lisbeth, Pedersen, Per A, Jorgensen, Peter L, Håkansson, Kjell O
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites Cloning, Molecular Crystallization - methods Membrane Proteins - chemistry Nickel Protein Structure, Tertiary Protein Subunits - chemistry Sodium-Potassium-Exchanging ATPase - chemistry Swine Thimerosal X-Ray Diffraction - methods
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Beschreibung
Zusammenfassung:	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 NiCl(2). The crystals belong to space group F23, with unit-cell parameters a = b = c = 147.5 A, and diffract to 3.1 A. 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.
ISSN:	0907-4449
DOI:	10.1107/S0907444903008795