The 11 A resolution projection map of Na+/K+-ATPase calculated by application of single particle analysis to two-dimensional crystal images.
Two-dimensional (2D) crystals of Na+/K+-ATPase were vitrified and observed with an electron cryo-microscope that allowed specimen observation at liquid helium temperature. Images showing 19 A spots on the optical diffraction patterns were digitized and processed by a crystallographic method. After optimization of parameters for the image processing, the locally averaged images revealed that each 2D crystal contained heterogeneous molecules. Single particle analysis was therefore applied to the 2D crystal images to select homogeneous molecule images, and averaging the selected images significantly improved map quality. Five major peak densities were clearly resolved in the new projection map, while two were found previously.
Tahara
Y
Y
Oshima
A
A
Hirai
T
T
Mitsuoka
K
K
Fujiyoshi
Y
Y
Hayashi
Y
Y
D000818:Animals; D020285:Cryoelectron Microscopy / Q000379:methods; D018360:Crystallography, X-Ray / Q000379:methods*; D004285:Dogs; D007679:Kidney Medulla / Q000201:enzymology; D008565:Membrane Proteins / Q000737:chemistry; D020836:Protein Structure, Quaternary; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry*
D008565:Membrane Proteins; D000254:Sodium-Potassium-Exchanging ATPase