Single-particle analysis can obtain 3D information not only from the crystals but also from the individual glycoprotein particles in thin ice (Fig. 1a) and can obtain atomic models in a relatively short period. This is because the interaction of electrons with atoms is 4–5 orders of magnitude larger than that of X-rays. In general, for the structural analysis of membrane proteins, the lipids/surfactants surrounding the transmembrane region along with the sugar chain is a major key. Chen et al. showed a ligand-binding structure at 3.0 Å by replacing the detergent (solubilizer) surrounding TRPVI with a lipid Nanodisc, bringing it closer to a natural phospholipid structure [1]. Structural polymorphism often corresponds to each snapshot when the protein moves to function. In the case of the PTH1 receptor involved in bone formation, five structures have been solved by cryo-electron microscopy, greatly advancing our understanding of its movement and mechanism [2].