STRUCTURAL BIOLOGY OF ENERGY-TRANSDUCING MEMBRANE PROTEINS

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 为了检验关于该蛋白质中铁-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，其中该结构域被晶体接触固定。这是我们以前使用的P6522晶体的情况（Zhang等人，Nature 1998 392：677-84;也是由另一个小组沉积的结构1BE 3）。现在我们正试图再次生长这些晶体并提高分辨率，但家庭来源是出于委员会，所以我们需要筛选以及收集在同步加速器。

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.