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The variable region of camelid heavy-chain antibodies produces the smallest known antibody fragment with antigen-binding capability (a V H H). The V H H R303 binds internalin B (InlB), a virulence factor expressed by the pathogen Listeria monocytogenes. InlB is critical for initiation of Listeria infection, as it binds a receptor (c-Met) on epithelial cells, triggering the entry of bacteria into host cells. InlB is surface-exposed and is required for virulence, hence a V H H targeting InlB has potential applications for pathogen detection or therapeutic intervention. Here, the expression, purification, crystallization and X-ray diffraction of R303 are reported. Crystals of R303 were obtained following in situ proteolysis with trypsin. Gel filtration and SDS-PAGE revealed that trypsin removed the C-terminal tag region of R303, facilitating crystal formation. Crystals of R303 diffracted to 1.3 Å resolution and belonged to the monoclinic space group P2 1 , with unit-cell parameters a = 46.4, b = 31.2, c = 74.8 Å , = 93.8 . The crystals exhibited a Matthews coefficient of 1.95 Å 3 Da À1 with two molecules in the asymmetric unit.