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

Authors :
Alexandre P. Kuzin
Tao Sun
Gregg V. Crichlow
Michiyoshi Nukaga
Kayoko Mayama
James R. Knox
Source :
Acta crystallographica. Section D, Biological crystallography. 57(Pt 12)
Publication Year :
2001

Abstract

The Escherichia coli OXA-1 oxacillinase, a beta-lactamase which provides resistance to beta-lactam antibiotics (penicillins and cephalosporins), has been crystallized. A member of the class D family of serine beta-lactamases, OXA-1 is especially active against the penicillins oxacillin and cloxacillin and is now found in 10% of E. coli clinical isolates. Crystals grown from PEG 8000 at pH 7.5 diffract to 1.5 A resolution at 100 K and have space group P1 (Z = 2), with unit-cell parameters a = 36.0, b = 51.6, c = 72.9 A, alpha = 70.2, beta = 84.1, gamma = 81.5 degrees.

Details

ISSN :
09074449
Volume :
57
Issue :
Pt 12
Database :
OpenAIRE
Journal :
Acta crystallographica. Section D, Biological crystallography
Accession number :
edsair.doi.dedup.....6ec6f5a1edfd00fc3f3f038d90a07ef3