Researchers applied MINFLUX super‑resolution microscopy to resolve the subunit architecture and three‑dimensional orientation of cardiac ryanodine receptors (RyR) inside living cells. The study provides molecular‑scale maps of RyR assemblies that underpin excitation–contraction coupling in cardiomyocytes. MINFLUX combines minimal photon flux with nanometer precision to visualize protein organization at near‑molecular resolution; these new structural insights could inform rational design of RyR‑targeting therapeutics for arrhythmia and heart failure. Structural biologists and cardiovascular drug developers should consider MINFLUX data when prioritizing binding sites and mechanism‑based modulators.