was not possible in cryo-TEM as the droplets were too large for the electron beam to penetrate. With common labscale emulsification methods such as colloid mills, microfluidizers, and high-pressure homogenizers, polydisperse emulsions are obtained in which the diameter of droplets ranges from 200 nm to 10 µm. Unfortunately, the fluorescence signal of droplets, that would be small enough to be resolved in cryo-TEM, is too weak to be detected in the presence of large droplets. In cryo-FM, only bright 200 nm beads, but no small droplets, were detectable (Fig. ). This limitation calls for a sample preparation procedure where, for polydisperse emulsions, small droplets are separated from larger ones. Such a procedure would rely on the assumption that emulsifier composition at the interface is not perturbed by a mild separation procedure. This assumption is typically valid in case of food emulsions in which emulsifiers are kinetically trapped at the interface . Another assumption of adopting such a procedure would be that small droplets have a similar coverage of proteins as larger ones. Alternatively, microfluidic emulsification can be used since it provides monodisperse emulsions (ten . In recent pre-printed work , we observed different protein oxidation behaviour at droplet interfaces for emulsions prepared with microfluidic emulsification and conventional emulsification using a colloid mill. This finding could be explained by different arrangements of protein emulsifier at droplet interfaces. Such experimental manipulation of emulsifier arrangement opens an experimental route to deploy our cryo-CLEM workflow to investigate relation between protein coverage of droplet interfaces and the interplay of lipid and protein oxidation.