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

研究成果: Article査読

16 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)635-637
ページ数3
ジャーナルJournal of Molecular Biology
238
4
DOI
出版ステータスPublished - 1994 5 12
外部発表はい

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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