Abstract
An archaeal-type phosphoenolpyruvate carboxylase (PepcA) from Clostridium perfringens has been expressed in Escherichia coli in a soluble form with an amino-terminal His tag. The recombinant protein is enzymatically active and two crystal forms have been obtained. Complete diffraction data extending to 3.13 angstrom resolution have been measured from a crystal soaked in KAu(CN)(2), using radiation at a wavelength just above the Au L(III) edge. The asymmetric unit contains two tetramers of PepcA.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Clostridium perfringens / enzymology*
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Crystallization
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Crystallography, X-Ray
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Isoenzymes / chemistry
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Isoenzymes / genetics
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Molecular Sequence Data
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Phosphoenolpyruvate Carboxylase / chemistry*
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Phosphoenolpyruvate Carboxylase / genetics
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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X-Ray Diffraction
Substances
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Archaeal Proteins
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Bacterial Proteins
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Isoenzymes
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Recombinant Proteins
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Phosphoenolpyruvate Carboxylase