STRUCTURE DETERMINATION OF BACTERIOPHAGE P22 TAIL FACTOR GP26

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。我们已经成功地从噬菌体P22中结晶出了尾部因子gp26。从最近解决的整个病毒尾巴的冷冻电镜重建中，我们知道gp26是一种细长的蛋白质，它可能形成从噬菌体尾部伸出的针或“注射装置”。我们最近（在斯坦福大学）在一些壮观的gp26晶体上收集了漂亮的2A原生数据。初步的晶体学分析表明，gp26可能形成一个非常细长的六聚体。这个单体只有25Kda， 95%是螺旋状的，这表明gp26可能会形成一种新型的病毒六螺旋束结构。我们确实需要光束时间来相位这个美丽的分子。作为一种替代方法，我想收集小角度x射线散射数据，以获得Gp26的低分辨率包络，这可能与6倍ncs一起使用，以相位低聚物。

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.