AbstractTwo-dimensional crystals of membrane-bound Na+,K+-ATPase were formed in acidic media and their qualities were investigated by electron cryo-microscopy as well as by conventional electron microscopy. At pH 4.8 in sodium citrate buffer, the best crystallization condition, more than 80% of membranes formed crystals. The high ratio allowed high-resolution images to be taken by electron cryo-microscopy. Image processing revealed that they had unique lattice constants (a = 108.7 Å, b = 66.2 Å, γ = 104.2°) and had few defects in the crystalline arrays. The reconstituted Fourier map of the ice-embedded crystal showed that there are two high contrast parts in one unit cell
AbstractA variant form of the Kdp-ATPase of Escherichia coli was overproduced to a level approaching...
AbstractBy using Bio-Beads as a detergent-removing agent, it has been possible to produce detergent-...
ABSTRACT Obtaining large, flat, well ordered crystals represents the key to structure determination ...
AbstractProlonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2...
AbstractThe three-dimensional structure of Na,K-ATPase was determined by electron microscopy and ima...
AbstractIon channels and pumps in cell membranes consist of multiple transmembrane segments that are...
The molecular structure of Na,K-ATPase was determined by electron crystallography from two-dimension...
Electron microscopy and two-dimensional crystallography have been used to study the molecular struct...
AbstractTwo-dimensional membrane crystals of renal Na,K-ATPase were analyzed by electron microscopy ...
Na$^+$,K$^+$-ATPase is responsible for the transport of Na$^+$ and K$^+$ across the plasma membrane ...
Obtaining large, flat, well ordered crystals represents the key to structure determination by electr...
In an attempt to better define the parameters governing reconstitution and two-dimensional crystalli...
Large, well-ordered 2-D crystals of the dodecylmaltoside complex of the Neurospora crassa plasma mem...
AbstractTreatment of purified preparations of porcine Na+,K+-ATPase with phospholipase A2, MgCl2 and...
The isolated membrane-bound enzyme retains its ouabain-sensitive ATP hydrolysis activity, and produc...
AbstractA variant form of the Kdp-ATPase of Escherichia coli was overproduced to a level approaching...
AbstractBy using Bio-Beads as a detergent-removing agent, it has been possible to produce detergent-...
ABSTRACT Obtaining large, flat, well ordered crystals represents the key to structure determination ...
AbstractProlonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2...
AbstractThe three-dimensional structure of Na,K-ATPase was determined by electron microscopy and ima...
AbstractIon channels and pumps in cell membranes consist of multiple transmembrane segments that are...
The molecular structure of Na,K-ATPase was determined by electron crystallography from two-dimension...
Electron microscopy and two-dimensional crystallography have been used to study the molecular struct...
AbstractTwo-dimensional membrane crystals of renal Na,K-ATPase were analyzed by electron microscopy ...
Na$^+$,K$^+$-ATPase is responsible for the transport of Na$^+$ and K$^+$ across the plasma membrane ...
Obtaining large, flat, well ordered crystals represents the key to structure determination by electr...
In an attempt to better define the parameters governing reconstitution and two-dimensional crystalli...
Large, well-ordered 2-D crystals of the dodecylmaltoside complex of the Neurospora crassa plasma mem...
AbstractTreatment of purified preparations of porcine Na+,K+-ATPase with phospholipase A2, MgCl2 and...
The isolated membrane-bound enzyme retains its ouabain-sensitive ATP hydrolysis activity, and produc...
AbstractA variant form of the Kdp-ATPase of Escherichia coli was overproduced to a level approaching...
AbstractBy using Bio-Beads as a detergent-removing agent, it has been possible to produce detergent-...
ABSTRACT Obtaining large, flat, well ordered crystals represents the key to structure determination ...