Abstract
Geranylgeranyl diphosphate (GGPP) synthase from Thermus thermophilus HB8 was expressed in Escherichia coli, purified to homogeneity and crystallized both as the recombinant native protein and its selenomethionine (SeMet) derivative. Well diffracting crystals of these proteins were obtained belonging to the tetragonal space group P4(1) or P4(3), with unit-cell parameters a = b = 139.88, c = 73.37 A. There were two homodimers in the asymmetric unit. A native data set was collected to 1.55 A resolution and a data set suitable for MAD phasing was collected to 2.40 A resolution on beamline BL40B2 at SPring-8.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alkyl and Aryl Transferases / chemistry*
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Alkyl and Aryl Transferases / genetics
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Alkyl and Aryl Transferases / isolation & purification
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Base Sequence
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Chromatography, Gel
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Crystallization
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Crystallography, X-Ray
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DNA, Bacterial / chemistry
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DNA, Bacterial / genetics
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Escherichia coli / genetics
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Geranylgeranyl-Diphosphate Geranylgeranyltransferase
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Molecular Sequence Data
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Polymerase Chain Reaction
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Sequence Analysis, DNA
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Thermus thermophilus / enzymology*
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Thermus thermophilus / genetics
Substances
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Bacterial Proteins
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DNA, Bacterial
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Recombinant Proteins
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Alkyl and Aryl Transferases
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Geranylgeranyl-Diphosphate Geranylgeranyltransferase