铜绿假单胞菌感染的治疗一直是低免疫力人群的难题，WbpM蛋白是铜绿假单胞菌O抗原合成的关键蛋白，参与形成铜绿假单胞菌的毒力因子脂多糖。冷冻电镜技术广泛应用于生物大分子结构的解析，具有辐射损伤小，无需结晶等优点。本文利用大肠杆菌感受态细胞DH5α过表达WbpM蛋白，对该蛋白进行纯化，最终获得了该蛋白纯度较高样品。依靠该样品进行了冷冻电镜实验，成功获得了WbpM蛋白单颗粒的冷冻电镜图，这为WbpM蛋白结构解析与功能的进一步阐释提供了方法，并且对铜绿假单胞菌感染的治疗提供了新的思路。

The treatment of Pseudomonas aeruginosa infection has always been a challenge for people with low immunity. WbpM protein is a key protein in the synthesis of Pseudomonas aeruginosa O antigen and is involved in the formation of the virulence factor lipopolysaccharide of Pseudomonas aeruginosa. Freezing electron microscopy technology is widely used in the analysis of biological macromolecular structures, with advantages such as minimal radiation damage and no need for crystallization. This article utilizes Escherichia coli competent cell DH5α overexpressing the WbpM protein, purifying the protein, and ultimately obtaining a high purity sample of the protein. Based on this sample, cryo electron microscopy experiments were conducted and the cryo electron microscopy images of WbpM protein single particles were successfully obtained. This provides a method for further elucidating the structure and function of WbpM protein, and provides new ideas for the treatment of Pseudomonas aeruginosa infection.