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Structural studies of cytochrome<jats:italic>bc<\/jats:italic><jats:sub>1<\/jats:sub>from mammalian homologues co-crystallized with lead compounds have underpinned structure-based drug design to develop compounds with higher potency and selectivity. However, owing to the limited amount of cytochrome<jats:italic>bc<\/jats:italic><jats:sub>1<\/jats:sub>that may be available from parasites, all efforts have been focused on homologous cytochrome<jats:italic>bc<\/jats:italic><jats:sub>1<\/jats:sub>complexes from mammalian species, which has resulted in the failure of some drug candidates owing to toxicity in the host. Crystallographic studies of the native parasite proteins are not feasible owing to limited availability of the proteins. Here, it is demonstrated that cytochrome<jats:italic>bc<\/jats:italic><jats:sub>1<\/jats:sub>is highly amenable to single-particle cryo-EM (which uses significantly less protein) by solving the apo and two inhibitor-bound structures to \u223c4.1\u2005\u00c5 resolution, revealing clear inhibitor density at the binding site. 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