AN ULTRAHIGH RESOLUTION CRYSTAL STRUCTURE OF CTX-M BETA-LACTAMASE FOR ENZYME STU

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。 CTX-Mβ-内酰胺酶是近十年来在全球范围内出现的一组新的A类β-内酰胺酶。CTX-M酶的晶体衍射率低于ngstrom，从而可以确定交替构象和氢原子位置。这些信息对于确定催化残基的一般碱/酸作用和获得用于分子对接的准确蛋白质模板具有重要价值。之前在ALS Beamline 8.3.1上的实验受到像板大小的限制，我们无法收集低于0.85o的衍射数据。

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. CTX-M beta-lactamase is a new group of class A beta-lactamase that has emerged world-wide in the past ten years. The crystals of CTX-M enzymes diffract to sub-¿ngstrom resolution, permitting the determination of alternate conformations and hydrogen atom positions. Such information is of great value to identifying general base/acid roles for catalytic residues and to obtaining an accurate protein template for molecular docking. Previous experiments at ALS Beamline 8.3.1 were limited by the size of the image plate and we were not able to collect diffraction data below 0.85 ¿.