Tau is a soluble protein interacting with tubulin to stabilize microtubules. Under pathological conditions, it becomes hyperphosphorylated and adopts a filamentous conformation with a pivotal role in Alzheimer?s Disease pathogenesis. Although tau aggregation is an important marker of pathology, only little is known about its spatial and temporal profile, as the conventional biochemical techniques lack the necessary resolution and sensitivity for the characterization of its oligomeric species. My work focuses on establishing super resolution microscopy methodologies to study the aggregation of the tau protein at a single aggregate resolution. The established methodologies will enable the determination of the size and cellular location of tau aggregates, especially since these are highly heterogeneous in structure and typically smaller than the diffraction limit of light (~250 nm).