HIGH PRESSURE COOLING OF A CORYNEBACTERIUM DIPHTHERIAE PILIN

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。 我们的目标是确定白喉棒状杆菌菌毛蛋白的结构。该结构将为其组装和内部异肽键的形成机制提供重要信息。到目前为止，我们已经生长了这种蛋白质的几个晶体，包括天然的和硒蛋氨酸取代的(SEMet)。它们的衍射率通常约为2.5？，偶尔会衍射至2？然而，糟糕的光斑质量和这些晶体的大单胞(~33x59x437)严重阻碍了我们获得可靠数据的尝试，即使在微焦点光束线上也是如此。在康奈尔大学的Sol M.Gruner教授和Chae Un Kim博士的合作下，我们想看看高压冷冻后这些晶体的斑点质量是否有所改善。如果成功，我们希望收集自然晶体和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.