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Indian J Biochem Biophys. 2011 Dec;48(6):395-8.

Preparation, crystallization and preliminary X-ray crystallographic analysis of OXA-23, a carbapenemase conferring widespread antibiotic resistance.

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Drug Resistance Proteomics Laboratory, Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin, Gyeonggido 449-728, Republic of Korea.


OXA-23, a class D carbapenemase that confers widespread antibiotic resistance hydrolyzes the beta-lactam rings of beta-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 A resolution using synchrotron radiation. The crystal of OXA-23 belonged to space group P4(1) with unit cell parameters a = 82.47, b = 82.47 and c = 172.01 A. Analysis of the packing density showed that the asymmetric unit probably contained two molecules with a solvent content of 73.64%.

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