Many protein crystals are distinguished by 3-D structures that contain well-ordered interpenetrating nanoporous and mesoporous solvent channels often 0.5-10 nm in diameter. [1] These channels provide a chemically heterogeneous and chiral environment that comprises 30-65 % of the total crystal volume with associated pore volumes and surface areas in the range of 0.9-3.6 mL g À1 and 800-3000 m 2 g À1 , respectively. [1][2][3] The use of protein crystals for materials applications has been traditionally restricted by their mechanical and chemical fragility; however the onset of simple cross-linking technology has significantly extended the scope for protein aggregates and crystals in catalysis and drug delivery, [4,5] separation science, [2,[6][7][8] and sensors. [9] In general, cross-linking is achieved by soaking the protein crystals in a 1-5 % aqueous glutaraldehyde solution containing a heterogeneous mixture of monomers and aldol-based oligomers of various lengths. [10] Reaction of these species with lysine residues results in a network of Schiff-base coupled intermolecular linkages to produce cross-linked protein crystals with high structural fidelity.[11] As a result, the glutaraldehyde-fixed crystals are physically robust, stable in organic solvents, and insoluble in water. Moreover, immersion of the cross-linked crystals in aqueous solutions of organic dyes, drugs, and antibiotics results in uptake of the guest molecules specifically within the solvent channels of the protein lattice. [12][13][14][15][16] Here, we extend the above strategies for the sequestration of metal ions and their reduction products within the solvent channels of glutaraldehyde cross-linked lysozyme single crystals. We note that a related approach, but involving cross-linked virus crystals, has been used recently to template the deposition of Pt/Pd nanoparticles. [17] Lysozyme is an enzyme with a single polypeptide chain consisting of 129 amino acids (M w = 14 600), and can be readily crystalized in various polymorphic forms. [18][19][20][21][22] Significantly, the tetragonal polymorph (space group P4 3 2 1 2) has discrete uni-directional solvent channels, 1 to 2.5 nm in diameter, which are aligned parallel to the crystallographic c axis.[23] Each channel is located in the centre of the unit cell, surrounded locally by four protein molecules, and constructed from an interlinked network of pores and cavities lined with aspartate and lysine residues.[24] Herein, we exploit this structural arrangement as an ordered 1-D intracrystalline reaction environment for the periodic organization and nanoscale confinement of plasmonic nanowires of Ag or Au. Arrays of metallic nanofilaments are produced within the protein crystals by in situ redox reactions involving photoreduction of sequestered Ag À by BH 4 À ions preorganized into the solvent channels. The resulting metalized protein crystals are physically robust, regular in external morphology, and uniform in size. Such materials represent a new class of hybrid monoliths with patterned nanostruc...