STRUCTURAL STUDIES ON PROTEINS, PEPTIDES AND ENZYMES OF IMPORTANCE IN BIONANOTEC

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。 在加州州立大学和几个主要的本科院校的研究涉及蛋白质，肽和酶的生物纳米技术，生物医学，环境和工业过程中的重要性的三维结构的测定。SSRL对光束时间的要求集中在收集细菌细胞色素c？的高分辨率衍射数据，来自黑腹果蝇的新的肌球蛋白折叠伴侣、酵母羰基还原酶突变体、参与硫还原的单半胱氨酸黄素蛋白NAD（P）H氧化还原酶、来自海栖栖热生菌的新的RNA保护酶TM 0159、与天然产物抑制剂复合的重组β-分泌酶、几种酶（复合物和突变体）和基于螺旋肽的生物沸石。在SSRL收集数据的愿望是基于我们对来自许多不同晶体的高质量，高分辨率衍射数据的需求，其中一些晶体对于传统的X射线源来说太小或太敏感。虽然大多数蛋白质结构可以通过分子置换来确定，但至少有一种需要准确的MAD数据收集。

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. Research in the California State University and several predominantly undergraduate institutions involves the determination of the 3-D structures of proteins, peptides and enzymes of importance in bionanotechnology, biomedicine, environmental and industrial processes. This request for beam time at SSRL focuses on the collection of high resolution diffraction data from bacterial cytochromes c?, a novel myosin folding chaperone from Drosophila melanogaster, yeast carbonyl reductase mutants, single cysteine flavoprotein NAD(P)H oxidoreductases involved in sulfur reduction, a novel RNA safeguard enzyme TM0159 from Thermatoga maritima, recombinant beta-secretase in complex with natural product inhibitors, several dehydrogenases (complexes and mutants), and bio-zeolites based on helical peptides. The desire to collect data at SSRL is based upon our need for high quality, high resolution diffraction data from a number of different crystals, some of which are either too small or sensitive for conventional x-ray sources. While the majority of protein structures can be determined by molecular replacement, at least one requires accurate MAD data collection.