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

16 引用 (Scopus)

抜粋

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.

元の言語English
ページ(範囲)635-637
ページ数3
ジャーナルJournal of Molecular Biology
238
発行部数4
DOI
出版物ステータスPublished - 1994 5 12

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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