title: Preparation of Ca(2+)-ATPase1a Enzyme from Rabbit Sarcoplasmic Reticulum.
abstract: The SERCA calcium ATPase, probably the most well-investigated membrane protein both from a biophysical and structural view, can be purified from native source in substantial quantities, making it a favorable target when conducting biochemical experiments and structure determination, e.g., by X-ray crystallography.
authors.affiliation: Department of Biomedicine, Aarhus University, Ole Worms Allé 6, 8000, Aarhus C, Denmark. jvm@biomed.au.dk.|Centre for Membrane Pumps in Cells and Disease, Danish National Research Foundation, Aarhus C, Denmark. jvm@biomed.au.dk.
authors.forename: Jesper V
authors.initials: JV
authors.lastname: Møller
authors.affiliation: Department of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.|Centre for Membrane Pumps in Cells and Disease, Danish National Research Foundation, Aarhus C, Denmark.
authors.forename: Claus
authors.initials: C
authors.lastname: Olesen
mesh_terms: D000818:Animals; D002118:Calcium / Q000737:chemistry; D018360:Crystallography, X-Ray; D008967:Molecular Biology / Q000379:methods*; D011487:Protein Conformation; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases / Q000737:chemistry / Q000302:isolation & purification*
chemical_list: D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases; D002118:Calcium
keywords: Membrane protein; Native source purification; SR calcium ATPase