Fig. 7: Role of charged residues in the catalytic site for the assembly process analyzed by LILBID-MS.
From: Bacterial F-type ATP synthases follow a well-choreographed assembly pathway

a In vitro assembly of α[WT] (light blue) with β[K159Q] mutant (dark blue) shows no significant formation of the αβ heterodimer, which we observe for the α[WT] and β[WT] (Fig. 1b). b The addition of the central stalk γε (dark and light green) does not lead to the formation of the desired α3β3γε complex. c In vitro assembled α[R363K] (light blue) and β[WT] (dark blue) revealed reduced αβ heterodimer assembly. d The biggest complex that is observed after addition of γε (dark and light green) is an α2β2γε subcomplex with charge states (−1 to −4). Source data are provided as a Source Data file.