Resistance to antibiotics is a major problem for the clinical management of infectious diseases, which are still a major cause of human mortality worldwide and resistance against all known classes of antibiotics has emerged. Subtilin belongs to a group of compounds known as Lanthionine antibiotics, to which bacterial resistance is uncommon and which show high activity against major clinical pathogens. Its mechanism of action involves peptide binding to the target membrane, followed by recognition of lipid II, membrane breach and cell death. It also exhibits inhibitory properties on cell wall synthesis leading to its subsequent cell wall degradation, which is achieved by sequestration of undecaprenyl pyrophosphate, an essential lipid II precursor. In this study we seek to determine the structure of the subtilin/lipid II and subtilin/undecaprenyl pyrophosphate complex assemblies.