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Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12.
J Mol Biol. 1994 May 13; 238(4):635-7.JM

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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Authors+Show Affiliations

Roh JH
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
Suzuki H
No affiliation info available
Kumagai H
No affiliation info available
Yamashita M
No affiliation info available
Azakami H
No affiliation info available
Murooka Y
No affiliation info available
Mikami B
No affiliation info available

MeSH

Amine Oxidase (Copper-Containing)CrystallizationCrystallography, X-RayEscherichia coli

Pub Type(s)

Journal Article

Language

eng

PubMed ID

8176752

Citation

Roh, J H., et al. "Crystallization and Preliminary X-ray Analysis of Copper Amine Oxidase From Escherichia Coli K-12." Journal of Molecular Biology, vol. 238, no. 4, 1994, pp. 635-7.
Roh JH, Suzuki H, Kumagai H, et al. Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12. J Mol Biol. 1994;238(4):635-7.
Roh, J. H., Suzuki, H., Kumagai, H., Yamashita, M., Azakami, H., Murooka, Y., & Mikami, B. (1994). Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12. Journal of Molecular Biology, 238(4), 635-7.
Roh JH, et al. Crystallization and Preliminary X-ray Analysis of Copper Amine Oxidase From Escherichia Coli K-12. J Mol Biol. 1994 May 13;238(4):635-7. PubMed PMID: 8176752.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12. AU - Roh,J H, AU - Suzuki,H, AU - Kumagai,H, AU - Yamashita,M, AU - Azakami,H, AU - Murooka,Y, AU - Mikami,B, PY - 1994/5/13/pubmed PY - 1994/5/13/medline PY - 1994/5/13/entrez SP - 635 EP - 7 JF - Journal of molecular biology JO - J Mol Biol VL - 238 IS - 4 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 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. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/8176752/Crystallization_and_preliminary_X_ray_analysis_of_copper_amine_oxidase_from_Escherichia_coli_K_12_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(84)71321-0 DB - PRIME DP - Unbound Medicine ER -