Crystallographic characterization and three-dimensional model of yeast Cu,Zn superoxide dismutase

Francesco Frigerio, Mattial Falconi, Giuseppina Gatti, Martino Bolognesi, Alessandro Desideri, Franco Marmocchi, Giuseppe Rotilio

Research output: Contribution to journalArticlepeer-review


The Cu, Zn superoxide dismutase from yeast was crystallized in the orthorhombic space group P21212 with unit cell dimension a=105.1 Å, b=142.2 Å, c=62.1 Å. The crystals grow in 25 mM citrate, 10 mM phosphate buffer pH 6.5, and 6% (W/V) polyethylene glycol, with a Vm of 3,4 Å3 /dalton, for two dimers/asymmetric unit. The crystals were unstable in the mother liquor, but were stabilized by transfer to a 35% polyethylene glycol solution. This crystalline form diffracts at high resolution and is suitable for determination of the atomic structure. The three dimensional structure of the yeast enzyme could be model-built by computer graphics techniques using the bovine enzyme atomic coordinates as template. The proposed model requires removal of some salt bridges and non equivalence of the metal-binding sites in the subunits, in line with reported functional properties of the yeast enzyme.

Original languageEnglish
Pages (from-to)677-681
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Apr 28 1989

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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