Fig. 2: Architecture of complex A displaying crosslinking of ACP = KS domains.

a Structure of complex A at 3.9 Å with a contour level of 0.088. Distances of key residues in select domains are shown to compare the conformation of each protomer. The homodimeric architecture provides two catalytic chambers housing the catalytic process. ACPs engage their catalytic domains in chambers 1 and 2. b Linear organization of each domain in respective MAS protomers, where L1-L5 are linkers 1 to 5. Two protomers comprise the structure in (a). c Coomassie brilliant blue stained 6% SDS-PAGE gel (Supplementary Fig. 45) depicting the outcome of crosslinking with 1. d Selected particle stacks from 2D classification. e FSC curve for complex A density map (Supplementary Figs. S8–S9). f Demonstration of ACPs crosslinked at KSs, revealing dual site-selective crosslinking with 1 (Fig. 1b).