Plasmodium parasites which cause the devastating disease malaria, are transmitted by mosquito bite and primarily infect the body’s erythrocytes. Malaria parasites extensively modify erythrocytes so they can avoid the human immune system and acquire plasma nutrients to proliferate rapidly and ensure transmission to the next host. Erythrocyte modification is performed by hundreds of effector proteins that are made by the parasite and then exported into the erythrocyte. To help export the effector proteins, the parasite surrounds itself with molecular gateways called PTEX which recognise and then extrude their cargo proteins into the erythrocyte across a vacuole membrane that envelops the intracellular parasite. PTEX is comprised of 5 different proteins as well as several accessory subunits. How the PTEX complexes recognise their protein cargoes and are organised at the parasite surface is not well understood. For example, are PTEX complexes randomly distributed around the parasite or are they organised into discrete, highly structured zones of export? As the intraerythrocytic parasites are very small, quantifying the organisation of macromolecular complexes at the parasite surface is difficult using standard fluorescence techniques. Super resolution methods such as Structured Illumination Microscopy (SIM) may help resolve the macromolecular organisation of PTEX and our findings using this approach will be presented.