Abstract
The aphA gene of Salmonella enterica sv. Typhimurium strain MD6001 was cloned in the multicopy plasmid pBluescript SK(-). The recombinant AphA protein was purified to homogeneity. The protein crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 112.4, b = 130.2, c = 139.6 A. Consistent with the self-rotation function, there are two tetramers in the asymmetric unit, indicating a solvent content of approximately 54%. The crystals are composed of biologically active AphA molecules.
MeSH terms
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Acid Phosphatase / biosynthesis*
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Acid Phosphatase / chemistry*
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Acid Phosphatase / genetics
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Amino Acid Sequence
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Crystallization
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Crystallography, X-Ray / methods
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Molecular Sequence Data
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Protein Structure, Quaternary
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Salmonella typhimurium / enzymology*
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Salmonella typhimurium / genetics
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Sequence Analysis, Protein
Substances
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Recombinant Proteins
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Acid Phosphatase