Crystallization and preliminary X-ray study of a recombinant cutinase from Fusarium solani pisi

J Mol Biol. 1990 Sep 20;215(2):215-6. doi: 10.1016/S0022-2836(05)80339-0.

Abstract

Recombinant cutinase from Fusarium solani pisi is expressed and excreted with very high yields in Escherichia coli cultures. Cutinase was crystallized at 20 degrees C using the vapour diffusion technique, with polyethylene glycol 6000 as precipitant. Best crystals were obtained at pH 7.0 with polyethylene glycol 6000 as precipitant. Best crystals were obtained at pH 7.0 with polyethylene glycol at 15 to 20%. They are monoclinic, with space group P2(1) and cell dimensions a = 35.1 A, b = 67.4 A, c = 37.05 A and beta = 94.0 degrees; they diffract beyond 1.5 A resolution. The asymmetric unit contains one molecule of 22,000 Da (Vm = 1.98 A3/Da; 38% water).

MeSH terms

  • Carboxylic Ester Hydrolases / chemistry*
  • Carboxylic Ester Hydrolases / ultrastructure
  • Cloning, Molecular
  • Crystallography
  • Escherichia coli
  • Fungal Proteins / chemistry
  • Fungal Proteins / ultrastructure
  • Fusarium / enzymology*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / ultrastructure
  • X-Ray Diffraction

Substances

  • Fungal Proteins
  • Recombinant Proteins
  • Carboxylic Ester Hydrolases
  • cutinase