The nuclear pore complex (NPC) exhibits structural plasticity and has only been characterized at local resolutions of up to 15 (A) for the cytoplasmic ring (CR).Here we present a single-particle cryo-electron microscopy (cryo-EM) structure of the CR from Xenopus laevis NPC at average resolutions of 5.5-7.9 (A),with local resolutions reaching 4.5 (A).Improved resolutions allow identification and placement of secondary structural elements in the majority of the CR components.The two Y complexes in each CR subunit interact with each other and associate with those from flanking subunits,forming a circular scaffold.Within each CR subunit,the Nup358-containing region wraps around the stems of both Y complexes,likely stabilizing the scaffold.Nup205 connects the short arms of the two Y complexes and associates with the stem of a neighboring Y complex.The Nup214-containing region uses an extended coiled-coil to link Nup85 of the two Y complexes and protrudes into the axial pore of the NPC.These previously uncharacterized structural features reveal insights into NPC assembly.