Perforin is an integral part of the immune synapse. Its monomers self-assemble into arc- and ring-shaped pores that insert into target cell membranes, perforating them and allowing the transport of granzymes into cells to trigger apoptosis. Between atomic force microscopy and electron microscopy, we have high resolution snapshots of the self-assembly process. These have demonstrated that the monomers diffuse freely until they self-assemble into short arcs that insert into the membrane and continue to grow into full pores. By fluorescently labelling perforin molecules and imaging their assembly on a supported lipid bilayer with total internal reflection fluorescence (TIRF) microscopy at a temporal resolution of tens of milliseconds, we aim to fill in the gaps between those snapshots and gain a more complete picture of the dynamics of perforin self-assembly.