Journal
STAR PROTOCOLS
Volume 3, Issue 3, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.xpro.2022.101623
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Funding
- German Research Foundation (DFG) [HE 2544/12-2]
- BioInMe [322977937/GRK2344]
- China Scholarship Council
- Medical Faculty of the University of Freiburg [2021/A3-Sch]
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This protocol describes the purification of intact and active ATPase from the model cyanobacterium Synechocystis sp. PCC 6803. The purification is based on the fusion of a 3xFLAG tag to the beta subunit. The enzymatic activity and purity of the ATPase are demonstrated using mass spectrometry, denaturing, and blue-native PAGE.
The FoF1 ATP synthase (ATPase) is one of the most important protein complexes in energy metabolism. The isolation of functional ATPase complexes is fundamental to address questions about its assembly, regulation, and functions. This protocol describes the purification of intact and active ATPase from the model cyanobacterium Synechocystis sp. PCC 6803. Basis for purification is a 3xFLAG tag fused to the beta subunit. The ATPase is enzymatically active and its purity is demonstrated using mass spectrometry, denaturing, and blue-native PAGE. For complete details on the use and execution of this protocol, please refer to Song et al. (2022).
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