The cryoEM structure of the PLY pore complex shows clearly the interactions of the secondary structure elements of neighboring protomers. The structure further shows how elements of secondary structure present in the soluble form refold and take on a completely different structure in the membrane. While the formation of the long membrane-inserted β-hairpins was predicted as such, no one could know or predict the exact structure of the β-strands and how they interact to form the membrane-perforating barrel. Other structural elements, including the inner α-barrel and the newly formed helix in domain 1, are entirely new. These elements are involved in inter- and intramolecular interactions in the pore complex. Even at 4.5 to 5 Å resolution there can be no reasonable doubt of their existence and interaction. Targeting these regions with newly developed drugs would be an elegant way to inhibit pore formation and infection, and thus an effective means of putting these pathogen out of action. We think that our discussion of this aspect of the PLY structure is reasonable and adequate.