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

doi:10.1006/jmbi.1994.1321

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

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	635-637
Number of pages	3
Journal	Journal of Molecular Biology
Volume	238
Issue number	4
DOIs	https://doi.org/10.1006/jmbi.1994.1321
Publication status	Published - 1994 May 12
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1006/jmbi.1994.1321

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

abstract = "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 {\AA}, b = 168·4 {\AA} and c = 81·6 {\AA}. The asymmetric unit contains one molecule of MAO, with a crystal volume per protein mass (V(m)) of 2·88 {\AA}3/Da and a solvent content of 58% by volume. The crystals diffract X-rays to a resolution limit of at least 2·7 {\AA} and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis.",

keywords = "Copper-amine oxidase, Crystallization, Escherichia coli, Monoamine oxidase, X-ray crystallography",

author = "Roh, {Jung Hyeob} and Hideyuki Suzuki and Hidehiko Kumagai and Mitsuo Yamashita and Hiroyuki Azakami and Yoshikatsu Murooka and Bunzo Mikami",

year = "1994",

month = may,

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doi = "10.1006/jmbi.1994.1321",

language = "English",

volume = "238",

pages = "635--637",

journal = "Journal of Molecular Biology",

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T1 - Crystallization and preliminary X-ray analysis of copper amine oxidase from escherichia coli K-12

AU - Roh, Jung Hyeob

AU - Suzuki, Hideyuki

AU - Kumagai, Hidehiko

AU - Yamashita, Mitsuo

AU - Azakami, Hiroyuki

AU - Murooka, Yoshikatsu

AU - Mikami, Bunzo

PY - 1994/5/12

Y1 - 1994/5/12

N2 - 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.

AB - 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.

KW - Copper-amine oxidase

KW - Crystallization

KW - Escherichia coli

KW - Monoamine oxidase

KW - X-ray crystallography

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JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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