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Crystallization and preliminary crystallographic characterization of the copper-containing amine oxidase from pea seedlings.
J Mol Biol. 1993 Jan 05; 229(1):243-5.JM

Abstract

The copper-containing amine oxidase from pea seedlings has been crystallized using lithium sulfate as precipitant at pH 5.2. The unit cell is orthorhombic, space group P2(1)2(1)2(1), with dimensions a = 89.3 A, b = 113.4 A, c = 199.0 A. The mass of the asymmetric unit is 131(+/- 13) kDa, consistent with independent evidence that the molecule has two approximately 66 kDa subunits. The crystals diffract to 2.5 A in a synchrotron X-ray beam.

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Authors+Show Affiliations

Vignevich V
Department of Inorganic Chemistry, University of Sydney, N.S.W., Australia.
Dooley DM
No affiliation info available
Guss JM
No affiliation info available
Harvey I
No affiliation info available
McGuirl MA
No affiliation info available
Freeman HC
No affiliation info available

MeSH

Amine Oxidase (Copper-Containing)CrystallizationFabaceaePlants, MedicinalX-Ray Diffraction

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8421305

Citation

Vignevich, V, et al. "Crystallization and Preliminary Crystallographic Characterization of the Copper-containing Amine Oxidase From Pea Seedlings." Journal of Molecular Biology, vol. 229, no. 1, 1993, pp. 243-5.
Vignevich V, Dooley DM, Guss JM, et al. Crystallization and preliminary crystallographic characterization of the copper-containing amine oxidase from pea seedlings. J Mol Biol. 1993;229(1):243-5.
Vignevich, V., Dooley, D. M., Guss, J. M., Harvey, I., McGuirl, M. A., & Freeman, H. C. (1993). Crystallization and preliminary crystallographic characterization of the copper-containing amine oxidase from pea seedlings. Journal of Molecular Biology, 229(1), 243-5.
Vignevich V, et al. Crystallization and Preliminary Crystallographic Characterization of the Copper-containing Amine Oxidase From Pea Seedlings. J Mol Biol. 1993 Jan 5;229(1):243-5. PubMed PMID: 8421305.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary crystallographic characterization of the copper-containing amine oxidase from pea seedlings. AU - Vignevich,V, AU - Dooley,D M, AU - Guss,J M, AU - Harvey,I, AU - McGuirl,M A, AU - Freeman,H C, PY - 1993/1/5/pubmed PY - 1993/1/5/medline PY - 1993/1/5/entrez SP - 243 EP - 5 JF - Journal of molecular biology JO - J Mol Biol VL - 229 IS - 1 N2 - The copper-containing amine oxidase from pea seedlings has been crystallized using lithium sulfate as precipitant at pH 5.2. The unit cell is orthorhombic, space group P2(1)2(1)2(1), with dimensions a = 89.3 A, b = 113.4 A, c = 199.0 A. The mass of the asymmetric unit is 131(+/- 13) kDa, consistent with independent evidence that the molecule has two approximately 66 kDa subunits. The crystals diffract to 2.5 A in a synchrotron X-ray beam. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/8421305/Crystallization_and_preliminary_crystallographic_characterization_of_the_copper_containing_amine_oxidase_from_pea_seedlings_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(83)71022-3 DB - PRIME DP - Unbound Medicine ER -