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

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Standard

Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein. / Haue, Lisbeth; Pedersen, Per A; Jorgensen, Peter L; Håkansson, Kjell O.

I: Acta crystallographica Section D: Structural biology , Bind 59, Nr. Pt 7, 07.2003, s. 1259-61.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Haue, L, Pedersen, PA, Jorgensen, PL & Håkansson, KO 2003, 'Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein', Acta crystallographica Section D: Structural biology , bind 59, nr. Pt 7, s. 1259-61.

APA

Haue, L., Pedersen, P. A., Jorgensen, P. L., & Håkansson, K. O. (2003). Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein. Acta crystallographica Section D: Structural biology , 59(Pt 7), 1259-61.

Vancouver

Haue L, Pedersen PA, Jorgensen PL, Håkansson KO. Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein. Acta crystallographica Section D: Structural biology . 2003 jul.;59(Pt 7):1259-61.

Author

Haue, Lisbeth ; Pedersen, Per A ; Jorgensen, Peter L ; Håkansson, Kjell O. / Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein. I: Acta crystallographica Section D: Structural biology . 2003 ; Bind 59, Nr. Pt 7. s. 1259-61.

Bibtex

@article{7296e7141af94e94aa041dd87e18536a,
title = "Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein",
abstract = "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.",
keywords = "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",
author = "Lisbeth Haue and Pedersen, {Per A} and Jorgensen, {Peter L} and H{\aa}kansson, {Kjell O}",
year = "2003",
month = jul,
language = "English",
volume = "59",
pages = "1259--61",
journal = "Acta Crystallographica Section D: Biological Crystallography",
issn = "2059-7983",
publisher = "International Union of Crystallography",
number = "Pt 7",

}

RIS

TY - JOUR

T1 - Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein

AU - Haue, Lisbeth

AU - Pedersen, Per A

AU - Jorgensen, Peter L

AU - Håkansson, Kjell O

PY - 2003/7

Y1 - 2003/7

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Binding Sites

KW - Cloning, Molecular

KW - Crystallization/methods

KW - Membrane Proteins/chemistry

KW - Nickel

KW - Protein Structure, Tertiary

KW - Protein Subunits/chemistry

KW - Sodium-Potassium-Exchanging ATPase/chemistry

KW - Swine

KW - Thimerosal

KW - X-Ray Diffraction/methods

M3 - Journal article

C2 - 12832778

VL - 59

SP - 1259

EP - 1261

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

SN - 2059-7983

IS - Pt 7

ER -

ID: 203907079