NDLI: Crystallization and data collection of the nucleotide-binding domain of Mg-ATPase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Håkansson, Kjell O. Curovic, Aida
Description	Country affiliation: Denmark Author Affiliation: Håkansson KO ( Department of Biology, University of Copenhagen, Denmark. kohakansson@bio.ku.dk)
Abstract	Understanding of how P-type ATPases work would greatly benefit from the elucidation of more high-resolution structures. The nucleotide-binding domain of Mg-ATPase was selected for structural studies because Mg-ATPase is closely related to eukaryotic Ca-ATPase and Na,K-ATPase while the nucleotide-binding domain itself has diverged substantially. Two fragments of Mg-ATPase were cloned in Escherichia coli and purified. The entire cytoplasmic loop (residues 367-673), consisting of the phosphorylation and nucleotide-binding domains, expressed well and was purified in large quantities. The smaller 19.5 kDa nucleotide-binding domain (residues 383-545) expressed less well but formed crystals that diffracted to a resolution of 1.53 A which will be used for molecular replacement.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
DOI	10.1107/S1744309109001419
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 3
Volume Number	65
Language	English
Publisher	Wiley
Publisher Date	2009-03-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Adenosine Triphosphatases Chemistry Ca(2+) Mg(2+)-atpase Escherichia Coli Proteins Escherichia Coli Enzymology Membrane Transport Proteins Nucleotides Metabolism Amino Acid Sequence Crystallization Crystallography, X-ray Molecular Sequence Data Protein Structure, Tertiary Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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