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Hydrophobins are small fungal proteins that form polymeric fibrils, known as rodlets. These rodlets form a matted coating on the surface of aerial structures like air-dispersed spores. The coating is extremely amphipathic, with an outward facing hydrophobic surface that “water-proofs” the spores. The coating is also extremely robust and is being considered for material science applications. Our structure of the monomeric hydrophobin from Neurospora crassa shows that it is made up entirely of beta structure (top right), forming a 4-stranded beta-barrel. The structure contains two very flexible loops (seen top left), which may play a role in fibril formation. The electrostatic surface properties of the EAS structure are also consistent with the amphipathic nature of the rodlets (bottom), and have allowed us to create a model for fibril formation (see below).