XRAY DIFFRACTION ANALYSES OF EF TU COMPLEXES & PECTATE LYASE COMPLEXES

工作重点将集中在收集X射线衍射数据上 与抗生素络合的延伸因子Tu单晶。 Ef-Tu-抗生素络合物的大晶体通常是孪晶。这个 孪晶可以手动分离，但碎片是 最小尺寸一般小于100微米，质量很差 与传统的X射线源发生衍射。经验告诉我们 展示了优秀的数据集，分辨率扩展 超过2.3 E，可以收集在EF-Tu-抗生素晶体上，这些晶体是 只有20微米厚。在接下来的一年里，努力将集中在 三种不同类型的Ef-Tu结合部位的测定 抗生素。其中包括克洛霉素家族、噻唑基。 多肽家族和四环素家族。归根结底， 抗生素结合部位的鉴定将阐明 这些抗生素的作用以及提供必要的原子 为合理设计更有效、毒性更低的产品奠定基础 抗生素。

Efforts will be focused on x-ray diffraction data collection on single crystals of elongation factor, Tu, complexed with antibiotics. Large crystals of EF-Tu-antibiotic complexes are usually twinned. The twinned crystals can be manually separated but the fragments are generally less than 100 microns in the smallest dimension and poorly diffracting with conventional x-ray sources. Experience has demonstrated that excellent data sets, with resolution extending beyond 2.3 E, can be collected on EF-Tu-antibiotic crystals that are only 20 microns thick. In the next year, efforts will be focused on determining the EF-Tu binding site of three different classes of antibiotics. These include the kirromycin family, the thiazolyl peptide family and the tetracycline family. Ultimately, the identification of antibiotic binding sites will elucidate the mode of action of these antibiotics as well as provide the necessary atomic foundation for the rational design of more effective, less toxic antibiotics.