Crystallization and preliminary X-ray study of OXA-1, a class D beta-lactamase

Citation
T. Sun et al., Crystallization and preliminary X-ray study of OXA-1, a class D beta-lactamase, ACT CRYST D, 57, 2001, pp. 1912-1914
Citations number
17
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
12
Pages
1912 - 1914
Database
ISI
SICI code
0907-4449(200112)57:<1912:CAPXSO>2.0.ZU;2-V
Abstract
The Escherichia coli OXA-1 oxacillinase, a beta -lactamase which provides r esistance to beta -lactam antibiotics (penicillins and cephalosporins), has been crystallized. A member of the class D family of serine beta -lactamas es, OXA-1 is especially active against the penicillins oxacillin and cloxac illin and is now found in 10% of E. coli clinical isolates. Crystals grown from PEG 8000 at pH 7.5 diffract to 1.5 Angstrom resolution at 100 K and ha ve space group P1 (Z=2), with unit-cell parameters a=36.0, b=51.6, c=72.9 A ngstrom, alpha =70.2, beta =84.1, gamma =81.5 degrees.