STRUCTURAL DETERMINATION OF LACTOSE PERMEASE IN DIFFERENT CONFORMATIONS

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。 本实验的目的是通过膜转运蛋白的主要促进剂超家族(MFS)的乳糖渗透酶(Lacy)来确定乳糖/H+共转运的机制。我们计划解决花边不同构象的结构，并提高现有晶体结构的分辨率和质量。为此，我们获得了不同花边底物复合体、突变体或同系物的晶体。我们需要筛选数百个晶体，然后在选定的晶体上进行疯狂实验。这需要经常使用同步辐射。

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. The goal of the experiment is to determine the mechanism of lactose/H+ symport by the lactose permease of E. coli (LacY), a paradigm for the Major Facilitator Superfamily (MFS) of membrane transport proteins. We plan to solve structures of different conformations of LacY and improve the resolution and quality of currently available crystal structure. For this we obtained crystals of different LacY substrates complexes, mutants, or homologues. We need to screen several hundred crystals and then perform MAD experiments on selected crystals. This requires regular access to synchrotron radiation