Crystallization and Preliminary Crystallographic Analysis of Recombinant Xenopus laevis Cu, Zn Superoxide Dismutase b

K. D. Carugo, C. Collyer, A. Coda, M. T. Carri, A. Battistoni, G. Bottaro, F. Polticelli, A. Desideri, M. Bolognesi

Research output: Contribution to journalArticle

Abstract

The recombinant Cu,Zn superoxide dismutase from the South African frog Xenopus laevis, expressed in E. coli, has been crystallized in a form suitable for high resolution crystallographic investigations. The crystals grow from polyethylene glycol solutions, at pH 6.0, 28° C, and belong to the orthorhombic space group P212121 with unit cell edges a = 73.33, b = 68.86, c = 59.73 Å, one protein dimer (32,000 Mr) per asymmetric unit. Diffraction data have been collected to 3.0 Å resolution, and a molecular replacement solution found for Xenopus laevis superoxide dismutase using the bovine enzyme as search model. The crystallographic R-factor corresponding to this solution is 0.412, in the 15.0-3.0 Å resolution range.

Original languageEnglish
Pages (from-to)1008-1011
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume194
Issue number3
DOIs
Publication statusPublished - Aug 16 1993

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

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