HIGH PRESSURE COOLING OF A CORYNEBACTERIUM DIPHTHERIAE PILIN

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。 我们的目的是确定白喉棒状杆菌菌毛蛋白的结构。该结构将提供其组装和内部异肽键形成机制的重要信息。到目前为止，我们已经生长了几种这种蛋白质的晶体，包括天然的和硒代蛋氨酸取代的（SeMet）。他们通常会在2.5美分左右，偶尔也会在2美分左右。然而，这些晶体的较差的光斑质量和较大的晶胞（~33 x 59 x 437）严重阻碍了我们获得可靠数据的尝试，即使是在微焦点光束线上。与Sol M教授合作。Gruner和康奈尔大学的Chae Un Kim博士，我们想看看这些晶体的斑点质量是否会在高压低温冷却后得到改善。如果成功，我们希望收集天然和SeMet晶体的完整数据集。

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 aim to determine the structure of a Corynebacterium diphtheriae pilin protein. The structure will provide important information on its assembly and the mechanism of internal isopeptide bond formation. We have so far grown several crystals of this protein, both native and selenomethionine-substituted (SeMet). They typically diffract to about 2.5 ¿ and occasionally to 2 ¿ . However, the poor spot qualities and the large unit cell (~33 x 59 x 437 ¿ ) of these crystals severely hampered our attempts to get reliable data even at a microfocus beam line. In collaboration with Prof. Sol M. Gruner and Dr. Chae Un Kim at Cornell, we would like see if the spot qualities of these crystals improve upon high-pressure crycooling. If successful, we would like to collect full datasets of both native and SeMet crystals.