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Purification, crystallization and preliminary X-ray diffraction study of a recombinant cytokinin oxidase from Zea mays.
Acta Crystallogr D Biol Crystallogr. 2004 Aug; 60(Pt 8):1500-1.AC

Abstract

Cytokinins are hormones that are involved in plant growth and development. They are irreversibly degraded by cytokinin oxidases/dehydrogenases, flavoenzymes which contain a covalently bound flavine adenine dinucleotide (FAD) cofactor. Cytokinin oxidase from Zea mays (ZmCKO1) was overexpressed in the yeast Yarrowia lipolytica, purified (molecular weight 69 kDa) and crystallized using the hanging-drop method. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 250.6, b = 50.6, c = 51.5 A, beta = 94.1 degrees. A complete data set has been collected at 100 K to 1.95 A resolution on an X-ray synchrotron source.

Authors+Show Affiliations

Kopecný D
Laboratoire de Biologie Cellulaire, INRA, Route de Saint-Cyr, 78026 Versailles CEDEX, France.
Briozzo P
No affiliation info available
Joly N
No affiliation info available
Houba-Hérin N
No affiliation info available
Madzak C
No affiliation info available
Pethe C
No affiliation info available
Laloue M
No affiliation info available

MeSH

CrystallizationCrystallography, X-RayGene ExpressionOxidoreductasesRecombinant ProteinsZea mays

Pub Type(s)

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

Language

eng

PubMed ID

15272190

Citation

Kopecný, David, et al. "Purification, Crystallization and Preliminary X-ray Diffraction Study of a Recombinant Cytokinin Oxidase From Zea Mays." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 8, 2004, pp. 1500-1.
Kopecný D, Briozzo P, Joly N, et al. Purification, crystallization and preliminary X-ray diffraction study of a recombinant cytokinin oxidase from Zea mays. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 8):1500-1.
Kopecný, D., Briozzo, P., Joly, N., Houba-Hérin, N., Madzak, C., Pethe, C., & Laloue, M. (2004). Purification, crystallization and preliminary X-ray diffraction study of a recombinant cytokinin oxidase from Zea mays. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 8), 1500-1.
Kopecný D, et al. Purification, Crystallization and Preliminary X-ray Diffraction Study of a Recombinant Cytokinin Oxidase From Zea Mays. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 8):1500-1. PubMed PMID: 15272190.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization and preliminary X-ray diffraction study of a recombinant cytokinin oxidase from Zea mays. AU - Kopecný,David, AU - Briozzo,Pierre, AU - Joly,Nathalie, AU - Houba-Hérin,Nicole, AU - Madzak,Catherine, AU - Pethe,Claude, AU - Laloue,Michel, Y1 - 2004/07/21/ PY - 2004/05/21/received PY - 2004/06/17/accepted PY - 2004/7/24/pubmed PY - 2005/2/19/medline PY - 2004/7/24/entrez SP - 1500 EP - 1 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 8 N2 - Cytokinins are hormones that are involved in plant growth and development. They are irreversibly degraded by cytokinin oxidases/dehydrogenases, flavoenzymes which contain a covalently bound flavine adenine dinucleotide (FAD) cofactor. Cytokinin oxidase from Zea mays (ZmCKO1) was overexpressed in the yeast Yarrowia lipolytica, purified (molecular weight 69 kDa) and crystallized using the hanging-drop method. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 250.6, b = 50.6, c = 51.5 A, beta = 94.1 degrees. A complete data set has been collected at 100 K to 1.95 A resolution on an X-ray synchrotron source. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15272190/Purification_crystallization_and_preliminary_X_ray_diffraction_study_of_a_recombinant_cytokinin_oxidase_from_Zea_mays_ DB - PRIME DP - Unbound Medicine ER -