The bacteria flagella motor (BFM) is a large (~11 MDa) complex nanomachine that is made up of dozens of copies of different protein subunits. These protein subunits assemble in a specific order to form a complex consisting of a rotor and stators. The stators function as ion channels, allowing the influx of cations across the bacterial cell membrane to drive rotation of the rotor, which in turn enables bacteria to swim. Assembly of the BFM begins firstly with the formation of a template, which consists of a ring of 26 copies of the protein FliF. Upon formation of the FliF template, other proteins can then assemble to form the other components of the BFM including the switch complex, which consists of multiple copies of the proteins FliG, FliM and FliN, and stators, composed of the proteins MotA and MotB. We are interested in understanding how the BFM is able to self-assemble at a molecular level and to do this, we aim to artificially build the BFM. In addition to using the biological FliF ring template, an artificial template synthesized using DNA origami will be used to initiate the assembly of the switch-complex proteins FliG, FliM and FliN. Templated formation of the complexes will be studied using a range of techniques including transmission electron microscopy and single molecule fluorescence (TIRF microscopy). Furthermore, we will be investigating the kinetics of templated assembly by specifically looking at the ability of FliG to polymerise on a range of linear DNA templates, using biolayer interferometry. These studies will not only further our understanding into how the BFM assembles at a molecular level but will also provide insight into the mechanism and kinetics of its assembly.