Curli are proteinaceous fibrous structures produced on the surface of many gram-negative bacteria. As a major constituent of the extracellular matrix, curli mediate interactions between the bacteria and its environment, and as such, curli play a critical role in biofilm formation. Curli fibers share biophysical properties with a growing number of remarkably stable and ordered protein aggregates called amyloid. Here we describe experimental methods to study the biogenesis and assembly of curli by exploiting their amyloid properties. We also present methods to analyze curli-mediated biofilm formation. These approaches are straightforward and can easily be adapted to study other bacterially produced amyloids.