STRUCTURE DETERMINATION OF BACTERIOPHAGE P22 TAIL FACTOR GP26

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We have managed to crystallize the tail factor gp26 from bacteriophage P22. From a recently solved cryo-em reconstruction of the entire viral tail we know that gp26 is an elongated protein, which is likely to form the needle, or `injecting device` sticking out of the phage tail. We recently collected (at Stanford) beautiful 2A native data on some spectacular gp26 crystals. Preliminary crystallographic analysis shows that gp26 is likely to form a very elongated hexamer. The monomer, only 25Kda, is 95% helical, which suggested the intriguing possibility that gp26 may form a novel class of viral six-helix bundle structure. We do need beamtime to phase this beautiful molecule. As an alternative approach I`d like to collect small-angle X-ray scattering data to obtain a low-resolution envelope of Gp26, which may be use - together with the 6-fold ncs - to phase the oligomer.