STRUCTURAL BIOLOGY OF ENERGY-TRANSDUCING MEMBRANE PROTEINS

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。 为了验证关于这种蛋白质中铁-硫结构域的移动性的假设，我们需要从晶体形式中收集数据，在这种形式中，这个结构域被晶体接触捕获不动。这就是我们以前使用的P6522晶体的情况(Zhang等人。自然1998 392：677-84；也是另一组沉积的结构1BE3。现在我们正试图再次生长这些晶体并提高分辨率，但主源已经失效，所以我们需要在同步加速器进行筛选和收集。

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. In order to test a hypothesis about mobility of the iron-sulfur domain n this protein, we need to collect data from a crystal form in which this domain is trapped immobile by crystal contacts. This is the case in the P6522 crystals which we used previously (Zhang et al. Nature 1998 392: 677-84; also structure 1BE3 deposited by another group. Now we are trying to grow these crystals again and improve the resolution, but the home source is out of commission so we need to screen as well as collect at the synchrotron.