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Title: Expression, purification, crystallization, and preliminary X-ray crystallographic analysis of OXA-17, an extended-spectrum {beta}-lactamase conferring severe antibiotic resistance

OXA-17, an extended-spectrum {beta}-lactamase (ESBL) conferring severe antibiotic resistance, hydrolytically inactivates {beta}-lactam antibiotics, inducing a lack of eradication of pathogenic bacteria by oxyimino {beta}-lactams and not helping hospital infection control. Thus, the enzyme is a potential target for developing antimicrobial agents against pathogens producing ESBLs. OXA-17 was purified and crystallized at 298 K. X-ray diffraction data from OXA-17 crystal have been collected to 1.85 A resolution using synchrotron radiation. The crystal of OXA-17 belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 48.37, b = 101.12, and c = 126.07 A. Analysis of the packing density shows that the asymmetric unit probably contains two molecules with a solvent content of 54.6%.
Authors:
; ; ; ;  [1]
  1. Myongji University, Drug Resistance Proteomics Laboratory, Department of Biological Sciences (Korea, Republic of)
Publication Date:
OSTI Identifier:
22121687
Resource Type:
Journal Article
Resource Relation:
Journal Name: Crystallography Reports; Journal Volume: 58; Journal Issue: 4; Other Information: Copyright (c) 2013 Pleiades Publishing, Ltd.; http://www.springer-ny.com; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ANTIBIOTICS; ANTIMICROBIAL AGENTS; ASYMMETRY; BACTERIA; CRYSTALLIZATION; CRYSTALLOGRAPHY; CRYSTALS; ENZYMES; LACTAMS; ORTHORHOMBIC LATTICES; PATHOGENS; PURIFICATION; RESOLUTION; SOLVENTS; SPACE GROUPS; SYNCHROTRON RADIATION; TEMPERATURE RANGE 0273-0400 K; X RADIATION; X-RAY DIFFRACTION