Crystallization and preliminary X-ray study of OXA-1, a class D beta-lactamase.
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.
Sun
T
T
Department of Molecular and Cell Biology, The University of Connecticut, Storrs, Connecticut 06269-3125, USA.
Nukaga
M
M
Mayama
K
K
Crichlow
G V
GV
Kuzin
A P
AP
Knox
J R
JR
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D014501:Uranium / Q000737:chemistry; D001618:beta-Lactamases / Q000737:chemistry*
D014501:Uranium; C039404:beta-lactamase OXA-2; D001618:beta-Lactamases