The rise of antimicrobial resistance has motivated the search for new classes of antibiotics. Synthetic exploration of antibiotic scaffolds is a proven strategy for enriching the therapeutic pipeline. Our laboratory has a programmatic focus on the development of new reactions for the syntheses of antibiotics with mechanisms of action distinct from ones which are FDA-approved. Bactobolin A is one such antibiotic which we were motivated to pursue, both for its broad-spectrum antibacterial activity and for its complex, functional-group rich scaffold (Figure ). Bactobolin A inhibits bacterial protein translation by binding to the L2 protein of the bacterial ribosome 50s subunit, which is an unusual location for antibiotic interactions. To date, there exists one racemic synthesis (Weinreb) and one enantiospecific synthesis (Švenda) of Bactobolin A (Figure ). Creative albeit unfinished approaches to Bactobolin A have been furnished by Danishefsky, Fraser-Reid, and Ward. There are only a few reports on the syntheses and analyses of Bactobolin A derivatives. Existing reports have focused on modifying Bactobolin A side chains rather than fundamentally altering the core scaffold. Based on our previous efforts with a model compound, we envisioned a synthesis of Bactobolin A in which our laboratory's sulfamate-tethered aza-Wacker cyclization would be used to install the 1,3-amino alcohol structural element. We hypothesized that such a route may also be amenable to furnishing unnatural isomers of Bactobolin A (Figure ) which would be difficult or impossible to access by chemical degradation or by semisynthetic studies with fermentation-derived natural product. Here, we describe our synthesis of key tricyclic intermediates using this strategy, which we envision can later be elaborated into Bactobolin A and interesting analogues.