Bacteriophages, viruses that infect bacteria, have evolved a variety of complex protein structures to carry their genomes between host cells. These proteins form the virion particle which can be considered a mostly self-assembled protein machine that protects the genome and effects genome entry into new cells. Because bacteriophages (phages) are often found in harsh environments including animal digestive tracts, sewage, and sea water, virion particle proteins are typically very stable and resistant to changes in pH, salts, digestive proteases, and other agents that typically denature or degrade proteins. Bacteriophage T4 long tail fibers are specialized proteins that bind to the host cell surface. They are very long (?160 nm) and thin (?3-5 nm) rigid fibrous multiprotein structures. The high length to width ratio of the long tail fibers (LTFs), rigidity, self-assembling properties plus chemical durability suggest that LTFs could be adapted into a self-patterning nanoscale protein structure or system. The long tail fibers of T4 are composed of 10 proteins, 3 copies each of gene product (gp) 34, gp 36, and gp 37 plus a single copy of gp 35 which forms the hinged ¿̐ưknee¿̐ư of the tail fiber. Although crystallizing whole tail fibers remains a challenge, other structural data on fiber fragments, related trimeric protein fibers, and other data suggest that some type of repetitive beta secondary structure comprise the rigid rod portions of the tail fibers.