Macromolecular X-Ray Crystallography Instrument

描述（由申请人提供）：宾夕法尼亚州立大学新成立的大分子x射线晶体学核心设施寻求资金购买最先进的x射线仪器：Rigaku Micromax 007HF x射线发生器，配备Varimax光学器件和R-AXIS HTC图像板探测器。该中心是哈克生命科学研究所的共享技术设施之一，将为整个大学公园校区提供服务。我们现有的Rigaku RU-200 x射线发生器是生物化学和分子生物学系的一部分，已有15年的历史。Rigaku目前在获得这种仪器的零件方面有困难。此外，现有发电机的通量是所要求发电机的十分之一。现有的R-Axis IV和R-Axis IV++探测器每张图像分别需要至少4分钟和2分钟。实际上，过去典型的晶体筛选和数据收集需要两到三周的时间，限制了2005年8月至12月期间大约10个数据集的使用。我们需要更高的x射线通量、更快的数据采集速度和更容易维护的x射线仪器。新的R-AXIS HTC探测器估计每张图像至少需要一分钟。使用Micromax 007HF的更高通量，我们预计数据收集时间将减少四倍或更多。有了这些优势，我们希望能够满足越来越多的研究人员对将大分子晶体学作为他们研究的一部分感兴趣的需要。我们有来自两个学院和四个系的17名教师参与了这次提案。其中12人是NIH资助的研究人员，3人正在等待NIH的提案。研究项目包括病毒蛋白、植物蛋白、蛋白质和核酸复合物以及金属酶。其中许多将有助于健康相关的研究。例如，对脊髓灰质炎病毒聚合酶突变体的结构研究可以为疫苗开发提供减毒RNA病毒的见解。总之，有了新的仪器，我们的目标是扩大大分子晶体学的研究，而不仅仅是生物化学和分子生物学部门的几个实验室。

DESCRIPTION (provided by applicant): The newly formed Macromolecular X-ray Crystallography Core Facility of the Pennsylvania State University seeks funds to purchase state-of-the-art X-ray instrumentation: Rigaku Micromax 007HF X-ray generator equipped with Varimax optics and R-AXIS HTC image plate detector. The center is one of the Shared Technology Facilities in the Huck Institute of the Life Sciences that will provide services to the entire University Park campus. Our existing Rigaku RU-200 X-ray generator is part of the Department of Biochemistry and Molecular Biology and is fifteen years old. Rigaku is currently having difficulty in getting parts for this instrument. Further, the flux of the existing generator is one-tenth that of the requested generator. The existing R-Axis IV and R-Axis IV++ detectors take a minimum of four and two minutes per image respectively. In reality typical crystal screening and data collection has taken two to three weeks in the past, limiting the use to about ten data sets between August and December of 2005. We need X-ray instrumentation with higher X-ray flux, faster data collection speed and easier maintenance. The new R-AXIS HTC detector is estimated to take a minimum of one minute per image. With the higher flux of Micromax 007HF, we expect the data collection times to reduce by a factor of four or more. With these advantages, we hope to meet the needs of the increasing number of investigators interested in incorporating macromolecular crystallography as part of their research. We have seventeen faculty members from two colleges and four departments participating in this proposal. Of these twelve are NIHfunded researchers and three have NIH proposals pending. The projects that will be addressed include viral proteins, plant proteins, complexes of proteins and nucleic acids and metallo-enzymes. Many of these will aid health related research. For example structural studies of poliovirus polymerase mutants could provide insight into attenuating RNA viruses for vaccine development. In conclusion, with the new instrumentation, our goal is to expand macromolecular crystallography research beyond just a few laboratories in the Department of Biochemistry and Molecular Biology.