Crystallization and preliminary X-ray diffraction analysis of monkey dimeric dihydrodiol dehydrogenase

Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):163-4. doi: 10.1107/s090744490101811x. Epub 2001 Dec 21.

Abstract

Dihydrodiol dehydrogenase catalyzes the NADP(+)-linked oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols and exists in multiple forms in mammalian tissues. The dimeric form of mammalian dihydrodiol dehydrogenase has a primary structure distinct from the previously known mammalian enzymes and may constitute a novel protein family with the prokaryotic proteins. Monkey kidney dimeric dihydrodiol dehydrogenase was crystallized from buffered ammonium phosphate solution using the hanging-drop vapour-diffusion method. The crystals diffract to 2.65 A resolution in the laboratory and belong to the hexagonal P6(1)22 or P6(5)22 space group, with unit-cell parameters a = b = 122.8, c = 121.3 A, alpha = beta = 90, gamma = 120 degrees.

MeSH terms

  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Dimerization
  • Macaca
  • Oxidoreductases / chemistry*
  • Protein Conformation
  • Recombinant Proteins / chemistry

Substances

  • Recombinant Proteins
  • Oxidoreductases
  • trans-1,2-dihydrobenzene-1,2-diol dehydrogenase