Hexagonal structure of two-dimensional crystals of the alpha 3 beta 3 complex thermophilic ATP synthase.
The highly dissociable alpha 3 beta 3 subunit complex (Mr = 319,582) of thermophilic ATP synthase was crystallized on a mercury surface under oxygen. The two-dimensional crystal was compared with that of TF1 (Mr = 385,351, alpha 3 beta 3 gamma delta epsilon subunit complex) by means of computer image processing. The crystals showed the same hexagonal lattice (a = b = 10 nm), despite the difference in their molecular weights. The color images of the two protein molecules were also hexagonal. However, there was an open hole in the image of the alpha 3 beta 3 complex, where small subunits (gamma, delta, and epsilon) of TF1 may have been located. The structure of this heterohexamer is consistent with that deduced from other physical parameters.
Yoshimura
H
H
Biometrology Laboratory, JEOL Ltd., Tokyo.
Endo
S
S
Matsumoto
M
M
Nagayama
K
K
Kagawa
Y
Y
D003460:Crystallization; D015394:Molecular Structure; D006180:Proton-Translocating ATPases
D006180:Proton-Translocating ATPases