biostudies-literatureUnknownCapper ENIGMS NIH HHSThe turbine dynamics of mitochondrial ATP synthases is an unresolved topic which in situ cryo-ET is poised to answer. Using publicly available tomogram data of vitrified Chlamydomonas reinhardtii cells, a monomer map of ATP synthase was refined to 6.67Å. With extensive heterogeneity analysis, we characterized the in situ conformation states of F1 head, central stalk, and upper peripheral stalk (UPS) individually, and analyzed the by-particle correlation between movement of the different domains, revealing the complex dynamics of the system within cells. While oligomycin sensitivity conferral protein (OSCP) and the UPS were found to bend with F1 head rotation, coupling between the rotation of central stalk and F1 head rotational states, suggested by previous in vitrobioRxiv : the preprint server for biology2025.09.10.674987https://www.ebi.ac.uk/biostudies/studies/S-EPMC12458427biostudies-literatureStructural dynamics of mitochondrial ATP synthase in Chlamydomonas reinhardtii revealed by in situ CryoET.PMC12458427R01 GM150905Capper EChen MfalseStructural dynamics of mitochondrial ATP synthase in Chlamydomonas reinhardtii revealed by in situ CryoET.The turbine dynamics of mitochondrial ATP synthases is an unresolved topic which in situ cryo-ET is poised to answer. Using publicly available tomogram data of vitrified Chlamydomonas reinhardtii cells, a monomer map of ATP synthase was refined to 6.67Å. With extensive heterogeneity analysis, we characterized the in situ conformation states of F1 head, central stalk, and upper peripheral stalk (UPS) individually, and analyzed the by-particle correlation between movement of the different domains, revealing the complex dynamics of the system within cells. While oligomycin sensitivity conferral protein (OSCP) and the UPS were found to bend with F1 head rotation, coupling between the rotation of central stalk and F1 head rotational states, suggested by previous in vitro2025-01-01T00:00:00Z2025 Sep2026-06-29T03:20:19.099Z2026-06-29T03:19:07.1ZS-EPMC124584274100100110.1101/2025.09.10.674987