CRYSTALLOGRAPHIC ANALYSIS OF A BACTERIAL MEMBRANE PROTEASE

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 本实验的目的是筛选IV型前胶原肽酶(TFPP)的晶体，TFPP是一种完整的膜蛋白，负责裂解细菌中的IV型前胶原。TFPP有8个跨膜螺旋。它只产生小尺寸的晶体(10？m厚)，并且在NSLS x29处表现出低分辨率的衍射。我们想用配备了微衍射仪的更高强度的光束线来测试这些晶体。我们能够充分利用24-ID-E光束线的特点，并获得了一些分辨率更高的衍射图像(尽管仍不足以进行结构确定)。根据我们从旅行中获得的信息，我们正在进一步改进结晶条件。

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.