PMID:8176752: Difference between revisions

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<span style = 'font-size: large'> '''Roh, JH, Suzuki, H, Kumagai, H, Yamashita, M, Azakami, H, Murooka, Y and Mikami, B'''  (1994) Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12.''J. Mol. Biol.'' '''238''':635-7</span>
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|{{TableHeadingColor}} |'''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 P2(1)2(1)2(1), with unit cell dimensions of a = 136.1 A, b = 168.4 A and c = 81.6 A. The asymmetric unit contains one molecule of MAO, with a crystal volume per protein mass (Vm) of 2.88 A3/Da and a solvent content of 58% by volume. The crystals diffract X-rays to a resolution limit of at least 2.7 A and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis.
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'''Roh, JH, Suzuki, H, Kumagai, H, Yamashita, M, Azakami, H, Murooka, Y and Mikami, B'''  (1994) Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12. ''J. Mol. Biol.'' '''238''':635-7
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!align=left  |Abstract
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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 P2(1)2(1)2(1), with unit cell dimensions of a = 136.1 A, b = 168.4 A and c = 81.6 A. The asymmetric unit contains one molecule of MAO, with a crystal volume per protein mass (Vm) of 2.88 A3/Da and a solvent content of 58% by volume. The crystals diffract X-rays to a resolution limit of at least 2.7 A and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8176752 PubMed]
Online version:[http://dx.doi.org/10.1006/jmbi.1994.1321 10.1006/jmbi.1994.1321]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8176752 PubMed]
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Amine Oxidase (Copper-Containing)/chemistry; Amine Oxidase (Copper-Containing)/isolation & purification; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology
 
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Latest revision as of 04:53, 15 September 2013

Citation

Roh, JH, Suzuki, H, Kumagai, H, Yamashita, M, Azakami, H, Murooka, Y and Mikami, B (1994) Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12. J. Mol. Biol. 238:635-7

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 P2(1)2(1)2(1), with unit cell dimensions of a = 136.1 A, b = 168.4 A and c = 81.6 A. The asymmetric unit contains one molecule of MAO, with a crystal volume per protein mass (Vm) of 2.88 A3/Da and a solvent content of 58% by volume. The crystals diffract X-rays to a resolution limit of at least 2.7 A and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis.

Links

PubMed Online version:10.1006/jmbi.1994.1321

Keywords

Amine Oxidase (Copper-Containing)/chemistry; Amine Oxidase (Copper-Containing)/isolation & purification; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology

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