STRUCTURAL GENOMICS OF CAENORHABDITIS ELEGANS

这个子项目是许多利用 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。 用X射线晶体学研究蛋白质折叠是现代结构生物学的基础。通常认为，功能相关的蛋白质形成有限数量的折叠家族，这些家族可以通过蛋白质晶体学和NMR的高通量方法来定位。梭elegans基因组，约19000个预测基因，提供了一个小的真核生物的结构研究的机会，并已被选定为结构基因组学东南合作实验室的目标。虽然在C.虽然我们已经发现了线虫蛋白质，但同步加速器光束时间的可用性仍然有限。我们提出了一系列的衍射实验，针对MAD/SAD相位的新的蛋白质结构从C。优雅大多数蛋白质将通过重原子试剂衍生化或作为硒代甲硫氨酸/硒代半胱氨酸变体产生。基于目前的生产，我们估计收集10-15种蛋白质的数据。

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. Exploration of protein folds by X-ray crystallography is a basis of modern structural biology. It is generally believed that functionally relevant proteins form a limited number of folding families which can be mapped by the high-throughput methods of protein crystallography and NMR. The C. elegans genome, with approximately 19000 predicted genes, provides opportunity for structural studies of a small eukaryotic organism and has been selected as a target by the Southeast Collaboratory for Structural Genomics. Although a significant progress has been made in production and crystallization of the C. elegans proteins, availability of the synchrotron beam time is still limited. We propose a series of diffraction experiments directed towards MAD/SAD phasing of the novel protein structures from C. elegans. A majority of the proteins will be either derivatized by heavy atom reagents or produced as selenomethionine/selenocysteine variants. Based on the current production, we estimate data collection for 10-15 proteins.