Two-dimensional crystals of the Kdp-ATPase of Escherichia coli.
A 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 A. This technique is a useful and simple method to obtain low-resolution structures of membrane proteins.
Iwane
A H
AH
Protein Engineering Research Institute, Suita, Osaka, Japan.
Ikeda
I
I
Kimura
Y
Y
Fujiyoshi
Y
Y
Altendorf
K
K
Epstein
W
W
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D027682:Cation Transport Proteins; D002462:Cell Membrane / Q000201:enzymology; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D005583:Fourier Analysis; D007091:Image Processing, Computer-Assisted; D007150:Immunohistochemistry; D008854:Microscopy, Electron; D014638:Vanadates
D002352:Carrier Proteins; D027682:Cation Transport Proteins; D029968:Escherichia coli Proteins; D014638:Vanadates; D000251:Adenosine Triphosphatases; C058166:potassium translocating Kdp-ATPase, E coli