The structure of the V-1-ATPase determined by three-dimensional electron microscopy of single particles

Autor(en): Radermacher, M
Ruiz, T
Wieczorek, H 
Gruber, G
Stichwörter: 3-DIMENSIONAL RECONSTRUCTION; ALIGNMENT; Biochemistry & Molecular Biology; Biophysics; Cell Biology; CTF correction; electron microscopy; ESCHERICHIA-COLI; F-1 ATPASE; F-1-ATPASE; H+V-ATPase; Manduca sexta; PROJECTIONS; RADON TRANSFORMS; RESOLUTION; simultaneous alignment; SUBUNIT; three-dimensional reconstruction; TILT SERIES; vacuolar-type ATPase
Erscheinungsdatum: 2001
Herausgeber: ACADEMIC PRESS INC ELSEVIER SCIENCE
Enthalten in: JOURNAL OF STRUCTURAL BIOLOGY
Band: 135
Ausgabe: 1
Startseite: 26
Seitenende: 37
Zusammenfassung: 
We determined the structure of the V-1-ATPase from Manduca sexta to a resolution of 1.8 nm, which for the first time reveals internal features of the enzyme. The V-1-ATPase consists of a headpiece of 13.5 nm in diameter, with six elongated subunits, A(3) and B-3, of approximately equal size, and a stalk of 6 nm in length that connects V-1 with the membrane-bound domain, V-O. At the center of the molecule is a cavity that extends throughout the length of the A(3)B(3) hexamer. Inside the cavity the central stalk can be seen connected to only two of the catalytic A subunits. The structure was obtained by a combination of the Random Conical Reconstruction Technique and angular refinements. Additional recently developed techniques that were used include methods for simultaneous translational rotational alignment of the 0 degrees images, contrast transfer function correction for tilt images, and the Two-Step Radon Inversion Algorithm. (C) 2001 Academic Press.
ISSN: 10478477
DOI: 10.1006/jsbi.2001.4395

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