Struture of the human ATP synthase (Molecular Cell)

Published: 31 March 2023| Version 1 | DOI: 10.17632/ykbbhdvvvy.1
Contributor:
Yuezheng Lai

Description

The origin data of PAGE, chromatography and activity measurement.

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Steps to reproduce

PAGE: Fractions from chromatography were mixed with native-page loading buffer (50%glycerol, 0.01%Ponceau) and conduct electrophoresis in Bis-Tirs 3-12% Native PAGE (Invitrogen) according to official protocol. Activity: Buffer contains 20mM Tris pH8.0, 150mM NaCl, 0.003%LMNG, 0.03%asolectin, 2mM MgCl2, 1mM phosphenol pyruvate, 2 units pyruvate kinase, 5 units lactate dehydrogenase, 0.2mM NADH, and 0.004mg/mL hATPase. Reaction was started by adding ATP to a final concentration of 2mM. For the inhibition group, oligomycin A (sigma) stocked in DMSO was added to a final concentration of 2 μM and control group was added with same volumne of DMSO.

Institutions

Nankai University

Categories

Cryo-Electron Microscopy, F-ATPase, Human

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