RESUMEN
OXA-23, a class D carbapenemase that confers widespread antibiotic resistance hydrolyzes the β-lactam rings of β-lactam antibiotics, presenting an enormous challenge to infection control, particularly in the eradication of pathogenic bacteria such as Acinetobacter baumannii, one of six top-priority dangerous pathogens. Thus, the enzyme is a potential target for developing antimicrobial agents against pathogens producing carbapenemases. In this study, OXA-23 was purified and crystallized at 298 K and X-ray diffraction data from OXA-23 crystal were collected at 2.03 Å resolution using synchrotron radiation. The crystal of OXA-23 belonged to space group P41 with unit cell parameters a = 82.47, b = 82.47 and c = 172.01 Å. Analysis of the packing density showed that the asymmetric unit probably contained two molecules with a solvent content of 73.64%.