AbstractProlonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2+, K+ and VO3− at 4°C resulted in formation of two-dimensional crystals of this enzyme with unit cell parameters: a = 66 Å, b = 118 Å, γ = 108°. The crystals correspond to the two-sided plane group p21. By combining tilted electron microscopic views of the crystals, a three-dimensional structure of (Na+ + K+)-ATPase was calculated at ~20 Å resolution. The unit cell is formed by two (αβ)-promoters which are in contact in their central parts. The structure was compared with chemical modification and immunochemical data; the arrangement of intra- and extramembrane domains was proposed
The isolated membrane-bound enzyme retains its ouabain-sensitive ATP hydrolysis activity, and produc...
AbstractTwo-dimensional crystals of membrane-bound Na+,K+-ATPase were formed in acidic media and the...
AbstractBy using Bio-Beads as a detergent-removing agent, it has been possible to produce detergent-...
AbstractProlonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2...
The molecular structure of Na,K-ATPase was determined by electron crystallography from two-dimension...
AbstractThe three-dimensional structure of Na,K-ATPase was determined by electron microscopy and ima...
Electron microscopy and two-dimensional crystallography have been used to study the molecular struct...
AbstractNa+,K+-ATPase is a heterodimer of α and β subunits and a member of the P-type ATPase family ...
AbstractTreatment of purified preparations of porcine Na+,K+-ATPase with phospholipase A2, MgCl2 and...
Na$^+$,K$^+$-ATPase is responsible for the transport of Na$^+$ and K$^+$ across the plasma membrane ...
AbstractTwo-dimensional membrane crystals of renal Na,K-ATPase were analyzed by electron microscopy ...
AbstractTwo-dimensional crystallization of membrane-bound H,K-ATPase (EC 3,6,1.36) in vesicle prepar...
AbstractTwo-dimensional crystals of the mitochondrial ATP synthase up to 0.4 μm in size were obtaine...
AbstractA variant form of the Kdp-ATPase of Escherichia coli was overproduced to a level approaching...
Large, well-ordered 2-D crystals of the dodecylmaltoside complex of the Neurospora crassa plasma mem...
The isolated membrane-bound enzyme retains its ouabain-sensitive ATP hydrolysis activity, and produc...
AbstractTwo-dimensional crystals of membrane-bound Na+,K+-ATPase were formed in acidic media and the...
AbstractBy using Bio-Beads as a detergent-removing agent, it has been possible to produce detergent-...
AbstractProlonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2...
The molecular structure of Na,K-ATPase was determined by electron crystallography from two-dimension...
AbstractThe three-dimensional structure of Na,K-ATPase was determined by electron microscopy and ima...
Electron microscopy and two-dimensional crystallography have been used to study the molecular struct...
AbstractNa+,K+-ATPase is a heterodimer of α and β subunits and a member of the P-type ATPase family ...
AbstractTreatment of purified preparations of porcine Na+,K+-ATPase with phospholipase A2, MgCl2 and...
Na$^+$,K$^+$-ATPase is responsible for the transport of Na$^+$ and K$^+$ across the plasma membrane ...
AbstractTwo-dimensional membrane crystals of renal Na,K-ATPase were analyzed by electron microscopy ...
AbstractTwo-dimensional crystallization of membrane-bound H,K-ATPase (EC 3,6,1.36) in vesicle prepar...
AbstractTwo-dimensional crystals of the mitochondrial ATP synthase up to 0.4 μm in size were obtaine...
AbstractA variant form of the Kdp-ATPase of Escherichia coli was overproduced to a level approaching...
Large, well-ordered 2-D crystals of the dodecylmaltoside complex of the Neurospora crassa plasma mem...
The isolated membrane-bound enzyme retains its ouabain-sensitive ATP hydrolysis activity, and produc...
AbstractTwo-dimensional crystals of membrane-bound Na+,K+-ATPase were formed in acidic media and the...
AbstractBy using Bio-Beads as a detergent-removing agent, it has been possible to produce detergent-...