Three-dimensional structure of (Na+ + K+ )-ATPase revealed by electron microscopy of two-dimensional crystals
نویسندگان
چکیده
منابع مشابه
The three-dimensional structure of the Na,K-ATPase from electron microscopy
The structure of Na,K-ATPase has been studied by electron microscopy and image reconstruction. A three-dimensional structure of this enzyme has been obtained to an overall resolution of 2.5 nm using data from specimens of negatively stained dimer sheets tilted through a range of angles +/- 60 degrees. The reconstruction shows a complex mass distribution consisting of ribbons of paired molecules...
متن کاملStructure of (Na+,K+)-ATPase as revealed by electron microscopy and image processing
(Na+,K+)-ATPase was studied by electron microscopy and image processing of negatively stained and freeze-dried and shadowed crystalline sheets induced by a number of inorganic salts. Extensive experiments have identified new conditions for optimum crystal formation. Two crystal forms have been observed, one with a monomer and the other with a dimer, in the unit cell. Both show the same structur...
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Two-dimensional crystals of the mitochondrial ATP synthase up to 0.4 microns in size were obtained from the detergent-lipid-protein micelles by detergent dialysis. A projected map of the negatively stained crystal was calculated from electron microscopical images by the Fourier-filtering procedure at about 2.8 nm resolution. The unit cell (with not more than two ATP synthase molecules) has the ...
متن کاملThree-dimensional structure of the KdpFABC complex of Escherichia coli by electron tomography of two-dimensional crystals.
The KdpFABC complex (Kdp) functions as a K+ pump in Escherichia coli and is a member of the family of P-type ATPases. Unlike other family members, Kdp has a unique oligomeric composition and is notable for segregating K+ transport and ATP hydrolysis onto separate subunits (KdpA and KdpB, respectively). We have produced two-dimensional crystals of the KdpFABC complex within reconstituted lipid b...
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Image analysis of electron micrographs of thin-sectioned myosin subfragment-1 (S1) crystals has been used to determine the structure of the myosin head at approximately 25-A resolution. Previous work established that the unit cell of type I crystals of myosin S1 contains eight molecules arranged with orthorhombic space group symmetry P212121 and provided preliminary information on the size and ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1985
ISSN: 0014-5793
DOI: 10.1016/0014-5793(85)80430-0