STRUCTURAL DETERMINATION OF LACTOSE PERMEASE IN DIFFERENT CONFORMATIONS

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。 本实验的目的是探讨E.大肠杆菌（LacY），膜转运蛋白的主要易化因子超家族（MFS）的范例。我们计划解决LacY的不同构象的结构，并提高目前可用的晶体结构的分辨率和质量。为此，我们获得了不同的LacY底物复合物，突变体，或同系物的晶体。我们需要筛选几百个晶体，然后在选定的晶体上进行MAD实验。这就需要定期接触同步辐射

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