With the ongoing resolution revolution in cryoEM (Kühlbrandt, 2014), structures of macromolecular assemblies can now be determined at high resolution without crystals. This is proving especially useful for membrane proteins and membrane protein complexes (Allegretti et al., 2015; Gu et al., 2016; Hahn et al., 2016; Letts et al., 2016; Liao et al., 2013), which tend to be unstable and flexible, and often do not crystallize. In the case of CDC pore complexes, structure determination represents a particular challenge, because they consist of variable numbers of 30 to 50 monomers (Dang et al., 2005; Shatursky et al., 1999; Shepard et al., 1998), and hence are intrinsically inhomogeneous. This fact has so far precluded structure determination of the membrane-attached or membrane-inserted form at high resolution. By a rigorous screen of the detergents used for solubilisation and purification of the pore complex from cholesterol-containing liposomes we were able to isolate a suitably homogenous population. Exchanging the detergent against amphipols appeared to stabilize rings of uniform size, as an important prerequisite for high-resolution single-particle cryoEM. The number of monomers in the amphipol-stabilized complexes was higher than in the prepores or the pores imaged by cryoET, even though the liposomes were prepared in the same way. This means that either the number of subunits in the ring varies from one liposome preparation to another, or that the rings rearrange into a more stable form upon detergent solubilisation, which we consider more likely. Interestingly, an earlier, low-resolution cryoEM structure of PLY pores and prepores in lipid bilayers deduced that there were 31 ± 3 subunits in the prepore and 38 or 44 in the pore complex (Tilley et al., 2005), in good agreement with our findings. Since the PLY pores in our subtomogram averages were smaller, consisting of 34 rather than 42 subunits, it seems that the rings can grow in the membrane by incorporating further subunits. Apparently, complexes of 42 monomers are more stable than both larger and smaller rings. The inherent variability in ring size restricts the number of particles that can be averaged in any one class. Moreover, the large ring-shaped assemblies are easily distorted and rarely, if ever, perfectly circular, which limits the accuracy to which they can be aligned by image processing. Both factors constrain the attainable resolution of the cryoEM reconstruction.