M. Radermacher et al., The structure of the V-1-ATPase determined by three-dimensional electron microscopy of single particles, J STRUCT B, 135(1), 2001, pp. 26-37
We determined the structure of the V-1-ATPase from Manduca sexta to a resol
ution 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 s
talk 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 le
ngth of the A(3)B(3) hexamer. Inside the cavity the central stalk can be se
en connected to only two of the catalytic A subunits. The structure was obt
ained by a combination of the Random Conical Reconstruction Technique and a
ngular 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, a
nd the Two-Step Radon Inversion Algorithm. (C) 2001 Academic Press.