Abstract
A fragment of the Streptococcus pneumoniae PhtA gene product (residues 18-230) was cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 62.19, b = 35.9, c = 72.54 A, beta = 90.01 degrees. The crystals diffract X-rays to beyond 1.2 A resolution.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Crystallization
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Crystallography, X-Ray
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Escherichia coli / genetics
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Hydrolases / chemistry*
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Hydrolases / genetics
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Hydrolases / isolation & purification*
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / isolation & purification
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Protein Conformation
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Streptococcus pneumoniae / chemistry*
Substances
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Peptide Fragments
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Recombinant Proteins
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histidine triad protein
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Hydrolases