Expression, purification, crystallization and preliminary X-ray analysis of Aeromonas hydrophilia metallo-beta-lactamase.
The CphA metallo-beta-lactamase from Aeromonas hydrophilia has been expressed, purified and crystallized by the hanging-drop vapor-diffusion method using ammonium sulfate as the precipitant. The crystals exhibit orthorhombic symmetry (P2(1)2(1)2), with unit-cell parameters a = 40.75, b = 42.05, c = 128.88 A. There is one monomer in the asymmetric unit and the solvent content is estimated to be 44% by volume. A data set extending to 1.8 A has been measured.
Sharma
Nandini
N
Department of Medicinal Chemistry, Merck Research Laboratories, PO Box 2000, RY 50-105, Rahway, NJ 07065-0900, USA. nandini_sharma@merck.com
Toney
Jeffrey H
JH
Fitzgerald
Paula M D
PM
D016980:Aeromonas hydrophila / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014162:Transfection; D014961:X-Ray Diffraction; D001618:beta-Lactamases / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D001618:beta-Lactamases; C082063:cphA protein, Aeromonas hydrophila