CRYSTALLOGRAPHIC ANALYSIS OF A BACTERIAL MEMBRANE PROTEASE

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 中心，不一定是研究者的机构。 本实验的目的是筛选IV型前菌毛蛋白肽酶（TFPP）的晶体，TFPP是一种负责细菌中IV型前菌毛蛋白裂解的完整膜蛋白。 TFPP具有8个跨膜螺旋。 它只产生小尺寸的晶体（厚度<10微米），并在NSLS X29下显示出低分辨率的衍射。 我们希望在配备显微衍射仪的更高强度光束线上测试这些晶体。 我们能够充分利用24-ID-E光束线的特性，并获得了一些分辨率提高的衍射图像（尽管仍不足以进行结构测定）。 根据我们从旅行中获得的信息，我们正在进一步改善结晶条件。

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. The objective of the experiment is to screen crystals of type IV prepilin peptidase (TFPP), an integral membrane protein responsible for the cleavage of type IV prepilins in bacteria. TFPP has 8 transmembrane helices. It generated only small-size crystals (<10¿m thickness) and showed low-resolution diffraction at NSLS X29. We wanted to test these crystals at a higher intensity beamline equipped with a microdiffractometer. We were able to take full advantage of the features of 24-ID-E beamline and have obtained some diffraction images with improved resolution (although still insufficient to allow structural determination). Based on the information we obtained from the trip, we are in the process of making further improvement of crystallization conditions.