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。 CTX-M β-内酰胺酶是近十年来在世界范围内出现的一类新的A类β-内酰胺酶。 CTX-M酶的晶体可达到亚纳米分辨率，允许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/酸作用以及获得用于分子对接的准确蛋白质模板具有重要价值。 ALS Beamline 8.3.1之前的实验受到图像板尺寸的限制，我们无法收集低于0.85 <$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 ¿.