The disease of transthyretin (TTR) amyloidosis (ATTR) has been known since the 1960s, and during these past 60 or so years, there has been a sustained peri-od of steady discoveries that have led to the current model of ATTR pathogene-sis. More recent research has achieved major advances in both diagnostics and therapeutics for ATTR, which are having a significant impact on ATTR patients today. Aiding these recent achievements has been the remarkable ability of cryo-electron microscopy (EM) to determine high-resolution structures of amy-loid fibrils obtained from individual patients. Here, we will examine cryo-EM structures of transthyretin amyloid fibrils to explore the structural basis of re-cent monoclonal antibody therapies for ATTR, including ALXN-2220 and Co-ramitug; as well as to point out potential applications of this approach to other systemic amyloid diseases.