Hexagonal Structure of Two-Dimensional Crystals of the α3β3 Complex of Thermophilic ATP Synthase1

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Abstract
The highly dissociable α3β3 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, α3β3γδεβ3 subunit complex) by means of computer image processing. The crystals showed the same hexagonal lattice (a=6=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 α3β3 complex, where small subunits (γ, δ, and ε) of TF1 may have been located. The structure of this heterohexamer is consistent with that deduced from other physical parameters.