PHASING AND SOLVING THE CRYSTAL STRUCTURE OF A PORTION OF A STAU PROTEIN

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 STAU蛋白质的一个区域已经结晶，我已经获得了高达1.5埃的天然衍射。 我现在正试图利用I3 C（5-氨基-2，4，6-三碘代苯甲酸）或Hg（磷酸乙基汞）的异常信号来获得相位信息，这些信号已经渗入晶体中。 获得这种蛋白质以前未知的结构对于理解Stau介导的衰变机制非常重要，这是Lynne Maquat实验室研究的一种机制，我是博士后。 当STAU与其同源RNA靶结合时，这种机制以一种依赖性的方式有条件地降解mRNA，从而控制细胞中特定蛋白质的丰度。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. A region of the STAU protein has been crystallized and I have obtained native diffraction up to 1.5 angstroms. I am now trying to obtain phase information using the anomolous signal of either I3C (5-amino-2,4,6-triiodoisophthalic acid), or Hg (ethyl mercuric phosphate), which have been soaked into the crystals. Obtaining the previously unkown structure of this protein is very important to understanding the mechanism of Stau mediated decay, which is a mechanim studied in Lynne Maquat`s lab where I am a postdoc. This mechanism conditionally degrades mRNA in a translationally dependent manner when STAU is bound to its cognate RNA target, thus controlling that particular protein`s abundance in the cell.