Crystallization and preliminary X-ray analysis of copper amine oxidase from escherichia coli K-12

Jung Hyeob Roh, Hideyuki Suzuki, Hidehiko Kumagai, Mitsuo Yamashita, Hiroyuki Azakami, Yoshikatsu Murooka, Bunzo Mikami

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Copper-containing monoamine oxidase (MAO) from Escherichia coli was overproduced in the periplasmic space by expression of the cloned gene. The purified MAO has been crystallized by means of the hanging drop technique using sodium citrate as a precipitant. The crystals belong to the orthorhombic system, space group P212121, with unit cell dimensions of a = 136·1 Å, b = 168·4 Å and c = 81·6 Å. The asymmetric unit contains one molecule of MAO, with a crystal volume per protein mass (V(m)) of 2·88 Å3/Da and a solvent content of 58% by volume. The crystals diffract X-rays to a resolution limit of at least 2·7 Å and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis.

Original languageEnglish
Pages (from-to)635-637
Number of pages3
JournalJournal of Molecular Biology
Issue number4
Publication statusPublished - 1994 May 12



  • Copper-amine oxidase
  • Crystallization
  • Escherichia coli
  • Monoamine oxidase
  • X-ray crystallography

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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