STRUCTURE DETERMINATION OF BACTERIOPHAGE P22 TAIL FACTOR GP26

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。我们已经成功地从噬菌体P22中结晶出尾部因子gp26。从最近解决的对整个病毒尾巴的冷冻电子显微镜重建中，我们知道gp26是一种拉长的蛋白质，很可能形成针，或从噬菌体尾巴伸出的注射装置。我们最近(在斯坦福大学)收集了一些壮观的gp26晶体的美丽的2a原生数据。初步的结晶学分析表明，gp26很可能形成一个非常细长的六角体。该单体只有25Kda，95%是螺旋的，这表明gp26可能形成一种新的病毒六螺旋束状结构。我们确实需要光束时间来定相这个美丽的分子。作为另一种方法，我想收集小角X射线散射数据，以获得Gp26的低分辨率包络，它可以与6倍的NCS一起使用来对低聚物进行相化。

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.