Figure 5.
Figure 5. Zipperlike structures observed in Δfcj1 mitochondria depend on the presence of dimer-specific Su e and Su g of F1FO–ATP synthase. Cryo-EM tomograms of isolated mitochondria of indicated strains. (A) Top views of putative F1FO–ATP synthases in Δfcj1/Δsu g mitochondria (left) and a surface-rendered representation (right) are shown. (B) Top views of putative F1FO–ATP synthases in Δfcj1 mitochondria (left; magnified view of boxed area in Fig. 4 E) and a surface-rendered representation (right) are shown. (C) Frequency distribution of F1–F1 distances. The center to center distance of an F1 particle to its nearest neighbor was determined for cryo-EM tomograms of isolated mitochondria of the indicated strains (n = 102 for both strains). Bars, 50 nm.

Zipperlike structures observed in Δfcj1 mitochondria depend on the presence of dimer-specific Su e and Su g of F1FO–ATP synthase. Cryo-EM tomograms of isolated mitochondria of indicated strains. (A) Top views of putative F1FO–ATP synthases in Δfcj1/Δsu g mitochondria (left) and a surface-rendered representation (right) are shown. (B) Top views of putative F1FO–ATP synthases in Δfcj1 mitochondria (left; magnified view of boxed area in Fig. 4 E) and a surface-rendered representation (right) are shown. (C) Frequency distribution of F1–F1 distances. The center to center distance of an F1 particle to its nearest neighbor was determined for cryo-EM tomograms of isolated mitochondria of the indicated strains (n = 102 for both strains). Bars, 50 nm.

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