Cross-linked protein crystals represent a new class of micro- and mesoporous materials with propertiespotentially useful in technologies as diverse as chiral separations and drug delivery. These applicationsrequire the generation of protein crystals in formats and sizes quite distinct from the traditionalsubmillimeter single crystals favored by structural biologists. Here we report a high-yield method forforming monodisperse protein crystals with tunable dimensions ranging from 250 nm up to tens ofmicrometers. X-ray powder diffraction of these crystallites confirms that the hen egg white lysozymecrystals are identical in structure to that of the bulk tetragonal lysozyme (a = 79.05 Å; c = 37.96 Å).