Expression, purification, crystallization and preliminary X-ray analysis of Aeromonas hydrophilia metallo-beta-lactamase

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt 2):180-2. doi: 10.1107/S1744309104033512. Epub 2005 Jan 8.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aeromonas hydrophila / enzymology*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / isolation & purification
  • Crystallography, X-Ray
  • Escherichia coli / enzymology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Transfection
  • X-Ray Diffraction
  • beta-Lactamases / chemistry*
  • beta-Lactamases / genetics*
  • beta-Lactamases / isolation & purification

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • beta-Lactamases
  • cphA protein, Aeromonas hydrophila