STRUCTURAL GENOMICS OF CAENORHABDITIS ELEGANS

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。 用X射线结晶学探索蛋白质折叠是现代结构生物学的基础。人们普遍认为，功能相关的蛋白质形成有限数量的折叠家族，这些折叠家族可以通过高通量的蛋白质结晶学和核磁共振方法进行定位。线虫基因组大约有19000个预测基因，为小型真核生物的结构研究提供了机会，并被东南结构基因组学合作实验室选为目标。尽管在线虫蛋白的生产和结晶方面已经取得了重大进展，但同步加速器束时间的可用性仍然有限。我们提出了一系列针对线虫新蛋白质结构的MAD/SAD相变的衍射实验。大多数蛋白质要么被重原子试剂衍生，要么以硒蛋氨酸/硒半胱氨酸变体的形式产生。根据目前的产量，我们估计收集的数据为10-15个蛋白质。

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.