Sea anemones produce a variety of toxic peptides and proteins, including many ion channel blockers and modulators, as well as potent cytolysins. This review describes the structures that have been determined to date for the major classes of peptide and protein toxins. In addition, established and emerging methods for structure determination are summarized and the prospects for modelling newly described toxins are evaluated. In common with most other classes of proteins, toxins display conformational flexibility which may play a role in receptor binding and function. The prospects for obtaining atomic resolution structures of toxins bound to their receptors are also discussed.