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Crystallization and preliminary X-ray study of OXA-1, a class D beta-lactamase
- 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.
- Subjects :
- Stereochemistry
medicine.drug_class
Protein Conformation
Antibiotics
Cephalosporin
medicine.disease_cause
Crystallography, X-Ray
beta-Lactamases
Microbiology
law.invention
Serine
Cloxacillin
Structural Biology
law
PEG ratio
polycyclic compounds
medicine
Escherichia coli
Crystallization
Chemistry
X-ray
General Medicine
biochemical phenomena, metabolism, and nutrition
Uranium
medicine.drug
Subjects
Details
- ISSN :
- 09074449
- Volume :
- 57
- Issue :
- Pt 12
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section D, Biological crystallography
- Accession number :
- edsair.doi.dedup.....6ec6f5a1edfd00fc3f3f038d90a07ef3