Ontology highlight
ABSTRACT:
SUBMITTER: Maeda S
PROVIDER: S-EPMC3855722 | biostudies-literature | 2013 Dec
REPOSITORIES: biostudies-literature
Maeda Shintaro S Shinzawa-Itoh Kyoko K Mieda Kaoru K Yamamoto Mami M Nakashima Yumiko Y Ogasawara Yumi Y Jiko Chimari C Tani Kazutoshi K Miyazawa Atsuo A Gerle Christoph C Yoshikawa Shinya S
Acta crystallographica. Section F, Structural biology and crystallization communications 20131129 Pt 12
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, ...[more]