JACK JOHNSON PRT-PRELIMINARY DATA COLLECTION ON P22 BACTERIOPHAGE

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 P22头-尾连接器（也称为门蛋白）是一种连接噬菌体P22的衣壳和尾部的寡聚锥形蛋白。 门蛋白也是将DNA泵入噬菌体头部的机器的组成部分。 寡聚体的每个亚基约为85.9KDa，预期寡聚体具有12倍旋转对称性，总大小约为1.1MDa。 我们已经在各种条件下获得了P22头-尾连接器的晶体，并在旋转阳极X射线发生器上测试了低温条件。 晶体的平均尺寸约为150*50*50 <$m3，具有完美的矩形形态。 我们希望收集一个高分辨率的数据集，并确定复杂的结构，通过使用低温EM低分辨率电子密度图作为起始模型。

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. P22 head-tail connector (also known as portal proteins) is an oligomeric cone-shaped protein that connects the capsid to the tail of bacteriophage P22. The portal protein is also an integral component of the machinery that pumps DNA into the phage head. Each subunit of the oligomer has approximately 85.9KDa and the oligomer is expected to have a 12-fold rotational symmetry with overall size of ~1.1MDa. We have obtained crystals of the P22 head-tail connector under various conditions and tested cryogenic conditions on a rotating anode x-ray generator. The crystals have an average size of ~150*50*50 ¿m3 and a perfect rectangular morphology. We hope to collect a high resolution data set and to determine the structure of the complex by using a cryo-EM low resolution electron density map as a starting model.