AbstractA variant form of the Kdp-ATPase of Escherichia coli was overproduced to a level approaching 37% of the protein in the inner membrane of this organism. Membranes from overproducing cells were prepared with an inside-out orientation. Incubation of the membranes on ice for 1–2 weeks in the presence of sodium vanadate resulted in the formation of two-dimensional crystals of the Kdp-ATPase. The calculated projection map of the p1 crystal form showed three prominent density peaks at a resolution of 22 Å. This technique is a useful and simple method to obtain low-resolution structures of membrane proteins
INTRODUCTIONAs recently as 10 years ago, the prospect of solving the structure of any membrane prote...
I. INTRODUCTIONMembrane proteins still present a major challenge in structural biology. Electron mic...
Electron microscopy and two-dimensional crystallography have been used to study the molecular struct...
AbstractA variant form of the Kdp-ATPase of Escherichia coli was overproduced to a level approaching...
Abstract2D crystallography has proven to be an excellent technique to determine the 3D structure of ...
Large, well-ordered 2-D crystals of the dodecylmaltoside complex of the Neurospora crassa plasma mem...
The solubilized surface protein of the Gram-negative bacterium Comamonas acidovorans was reconstitut...
AbstractDue to the difficulty to crystallize membrane proteins, there is a considerable interest to ...
Large single three-dimensional crystals of the dodecylmaltoside complex of the Neurospora crassa pla...
In an attempt to better define the parameters governing reconstitution and two-dimensional crystalli...
AbstractStructure determination at high resolution is actually a difficult challenge for membrane pr...
Challenges in the production of integral membrane proteins for structural studies include low expres...
AbstractProlonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2...
Membrane proteins play important roles for living cells. They control transportation of ions, solute...
Electron crystallography of two-dimensional crystals is a structure-determination method well suited...
INTRODUCTIONAs recently as 10 years ago, the prospect of solving the structure of any membrane prote...
I. INTRODUCTIONMembrane proteins still present a major challenge in structural biology. Electron mic...
Electron microscopy and two-dimensional crystallography have been used to study the molecular struct...
AbstractA variant form of the Kdp-ATPase of Escherichia coli was overproduced to a level approaching...
Abstract2D crystallography has proven to be an excellent technique to determine the 3D structure of ...
Large, well-ordered 2-D crystals of the dodecylmaltoside complex of the Neurospora crassa plasma mem...
The solubilized surface protein of the Gram-negative bacterium Comamonas acidovorans was reconstitut...
AbstractDue to the difficulty to crystallize membrane proteins, there is a considerable interest to ...
Large single three-dimensional crystals of the dodecylmaltoside complex of the Neurospora crassa pla...
In an attempt to better define the parameters governing reconstitution and two-dimensional crystalli...
AbstractStructure determination at high resolution is actually a difficult challenge for membrane pr...
Challenges in the production of integral membrane proteins for structural studies include low expres...
AbstractProlonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2...
Membrane proteins play important roles for living cells. They control transportation of ions, solute...
Electron crystallography of two-dimensional crystals is a structure-determination method well suited...
INTRODUCTIONAs recently as 10 years ago, the prospect of solving the structure of any membrane prote...
I. INTRODUCTIONMembrane proteins still present a major challenge in structural biology. Electron mic...
Electron microscopy and two-dimensional crystallography have been used to study the molecular struct...