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Electron microscopy (cryo-EM) is an essential tool to visualize proteins in near-native conditions. This is particularly true when dealing with heterogeneity—a hallmark of biological systems in health and disease. I will discuss how cryo-EM can uncover clinically relevant structural states using the membrane channel Pannexin-1 (PANX1) as a case study. PANX1 plays key roles in inflammation, ischemic injury, and immune cell activation due to its central role in ATP release. Yet, its regulation of the ATP-release state remains poorly understood. Using cryo-EM, we separated two PANX1 conformations and identified how phosphorylation stabilizes the open, large-pore state, enabling the passage of ATP and metabolites. This provides a structural basis for PANX1 activation in inflammatory and disease contexts. In a second example, cryo-EM allowed us to resolve compositional heterogeneity in a mixed protein sample, identifying three distinct structures—including one previously uncharacterized complex—at better than 3.5 Å. Together, these studies highlight cryo-EM’s power in deciphering biologically and clinically important complexity.
