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Title
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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.
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Authors
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D.Hasse,
M.Hagemann,
I.Andersson,
H.Bauwe.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010,
66,
187-191.
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PubMed id
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Abstract
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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.
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