Crystallization and preliminary X-ray analysis of polyamine oxidase from Zea mays L.

C. Binda, A. Coda, R. Angelini, R. Federico, P. Ascenzi, A. Mattevi

Research output: Contribution to journalArticle

Abstract

Polyamine oxidase catalyses the oxidation of the secondary amino group of spermine, spermidine and their acetyl derivatives. The enzyme plays an important role in the regulation of polyamine intracellular concentration and is a member of the family of flavin-containing amine oxidases. Crystals of maize polyamine oxidase have been grown by the hanging-drop vapour-diffusion technique. The crystals are in hexagonal space group P6122 (or P6522) with cell dimensions a = b = 184.6, c = 280.9 Å. A native data set has been collected to 2.7 Å resolution at a synchrotron radiation source.

Original languageEnglish
Pages (from-to)1429-1431
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue number6 II
DOIs
Publication statusPublished - Nov 1 1998

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

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