Brain dysfunction can be caused by aggregated proteins such as prions. In humans, the prion protein causes an infection by changing its shape and transforming into rope like aggregates. In this way, stable prion aggregates are immune to normal processes of destruction in an organism and bring about neuronal death and ultimately disease. There is no molecular explanation for the variable efficiency of prion spread between species. To investigate this phenomenon, STROBE scientists Rodriguez and Maio used cryo electron microscopy to reveal the atomic structures of regions within prion that have a high propensity to form structured aggregates. This made it possible to take an atomic look at structural motifs that may represent the molecular basis for a prion species barrier.