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Updated: May 5, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
Published on: January 22, 2019
Two-dimensional crystallization of intact F-ATP synthase isolated from bovine heart mitochondria
Shintaro Maeda1, Kyoko Shinzawa-Itoh, Kaoru Mieda
1Picobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori Akoh, Hyogo 678-1297, Japan.
Abstract:
Mitochondrial F-ATP synthase produces the majority of ATP for cellular functions requiring free energy. The structural basis for proton motive force-driven rotational catalysis of ATP formation in the holoenzyme remains to be determined. Here, the purification and two-dimensional crystallization of bovine heart mitochondrial F-ATP synthase are reported. Two-dimensional crystals of up to 1 µm in size were grown by dialysis-mediated detergent removal from a mixture of decylmaltoside-solubilized 1,2-dimyristoyl-sn-glycero-3-phosphocholine and F-ATP synthase against a detergent-free buffer. A projection map calculated from an electron micrograph of a negatively stained two-dimensional crystal revealed unit-cell parameters of a = 185.0, b = 170.3 Å, γ = 92.5°.
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