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Crystallization and preliminary X-ray diffraction analyses of the homodimeric glycine decarboxylase (P-protein) from the cyanobacterium Synechocystis sp. PCC 6803.
Department of Molecular Biology, Swedish University of Agricultural Sciences.
2010 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. 66, no Pt 2, 187-191 p.Article in journal (Refereed) Published
Abstract [en]

Glycine decarboxylase, or P-protein, is a major enzyme that is involved in the C(1) metabolism of all organisms and in the photorespiratory pathway of plants and cyanobacteria. The protein from Synechocystis sp. PCC 6803 is a homodimer with a mass of 215 kDa. Recombinant glycine decarboxylase was expressed in Escherichia coli and purified by metal-affinity, ion-exchange and gel-filtration chromatography. Crystals of P-protein that diffracted to a resolution of 2.1 A were obtained using the hanging-drop vapour-diffusion method at 291 K. X-ray diffraction data were collected from cryocooled crystals using synchrotron radiation. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 96.30, b = 135.81, c = 179.08 A.

Place, publisher, year, edition, pages
2010. Vol. 66, no Pt 2, 187-191 p.
National Category
Natural Sciences
Research subject
Biology with specialization in Structural Biology
Identifiers
URN: urn:nbn:se:uu:diva-292923DOI: 10.1107/S1744309109052828PubMedID: 20124719OAI: oai:DiVA.org:uu-292923DiVA: diva2:926976
Available from: 2016-05-10 Created: 2016-05-10 Last updated: 2016-05-12

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Hasse, Dirk
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