Understanding of cardiomyocyte subcellular structure has benefited greatly from the advent of sub-diffraction limit super resolution microscopy, particularly regarding the organization of Ryanodine Receptors (RyRs). These investigations have indicated that RyRs are present in clusters, and suggested that neighbouring clusters may cooperatively generate calcium sparks, the fundamental units of calcium release underlying the calcium transient. However, directly linking the structure of these RyR conformations to their function requires connecting super resolution imaging with calcium imaging. To this end, we presently employed cardiac myocytes isolated from mice expressing a photo-activated red fluorescent protein tagged ryanodine receptor 2 (PA-tag-RFP-RyR2). A commercial Zeiss Elyra dSTORM setup was used to image live PA-tag-RFP myocytes loaded with Fluo 4 calcium indicator. Calcium measurements were first obtained through HiLo illuminated widefield imaging, followed by PA light microscopy (PALM) imaging using the same camera setup. We observed that careful adjustment of the rate of fluorophore activation and photobleaching optimized the generation of blinking phenomena necessary for live cell PALM imaging. RyR localisation was obtained with accuracies of 30-40nm in the X, Y axis in live cell images, whereas somewhat higher resolution (5-15nm) was obtained in parallel experiments performed in fixed cells with RyR antibody labeling. RyR cluster arrangements were observed to be broadly consistent between the two imaging modalities. Spontaneous calcium sparks recorded in PA-tag-RFP-RyR2 myocytes were directly paired to underlying RyR constellations, allowing assessment of cooperative functional interactions between neighbouring RyR clusters. In ongoing work, this approach will quantitatively link calcium handling dynamics to the opening of individual RyRs, and allow real-time insight into the stochasticity and plasticity of this structure/function relationship.