Abstract
The crystallization and preliminary X-ray diffraction analysis of a catalytic domain of chitinase (PF1233 gene) from the hyperthermophilic archaeon Pyrococcus furiosus is reported. The recombinant protein, prepared using an Escherichia coli expression system, was crystallized by the hanging-drop vapour-diffusion method. An X-ray diffraction data set was collected at the undulator beamline BL44XU at SPring-8 to a resolution of 1.50 angstroms. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 90.0, b = 92.8, c = 107.2 angstroms.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Archaeal Proteins / chemistry
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Archaeal Proteins / isolation & purification
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Archaeal Proteins / metabolism
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Catalytic Domain
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Chitinases / chemistry*
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Chitinases / isolation & purification
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Chitinases / metabolism
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Cloning, Molecular
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Crystallization
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Escherichia coli / enzymology
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Molecular Sequence Data
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Pyrococcus furiosus / enzymology*
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Thermodynamics
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X-Ray Diffraction
Substances
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Archaeal Proteins
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Recombinant Proteins
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Chitinases