Sample vitrification and microscopy observation at low temperatures are especially helpful for food emulsions as cryogenic temperatures prevent the diffusion of components and further oxidation during measurements. Despite its apparent potential, Cryo-CLEM has not yet been employed for studying food systems. More specifically, the length scales covered by CLEM (nm to µm scale) have the potential to provide insights into the relationship between the (co-) oxidation of lipids and proteins at droplet interfaces and the local nanoscale arrangement of proteins. In previous work, we showed aggregation of proteins in the continuous phase separated from mayonnaise using localisation of fluorescently labelled spin-traps and autofluorescence by room temperature (RT)-confocal microscopy and cryo-TEM . We could observe aggregation of proteins in the aqueous phase upon oxidation, however, without employing fluorescence microscopy and cryo-TEM in a correlative manner.