Structure of two-dimensional crystals of membrane-bound Na,K-ATPase as analyzed by correlation averaging.
The structure of two-dimensional crystals of membrane-bound Na,K-ATPase from rabbit kidney has been analyzed with a correlation averaging procedure. Two principally different crystal forms are observed with p1 and p21 symmetry, respectively. In the p1 form the averaged projection structure shows a triangular shaped protein domain interpreted as a protomer (alpha beta-unit) of Na,K-ATPase. In the p21-form the stain-deficient area is extended toward a twofold symmetry axis. The results are in good agreement with a previous analysis where Fourier methods were applied to well ordered crystals of pig kidney Na,K-ATPase and illustrate that the correlation averaging procedure can be used for the analysis of membrane crystals of Na,K-ATPase showing curved lattice lines.
D000818:Animals; D007425:Intracellular Membranes / Q000201:enzymology* / Q000648:ultrastructure; D007679:Kidney Medulla / Q000201:enzymology* / Q000648:ultrastructure; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008861:Microsomes / Q000201:enzymology* / Q000648:ultrastructure; D011487:Protein Conformation; D011817:Rabbits; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D046911:Macromolecular Substances; D000254:Sodium-Potassium-Exchanging ATPase