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The peripheral stalk of the archaeal ATP synthase (A 1 A 0 )-ATP synthase is formed by the heterodimeric EH complex and is part of the stator domain, which counteracts the torque of rotational catalysis. Here we used nuclear magnetic resonance spectroscopy to probe the interaction of the C-terminal domain of the EH heterodimer (E CT1 H CT ) with the N-terminal 23 residues...
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