Abstract
Phosphoribosylglycinamide formyltransferase (PurN) from Streptococcus mutans was recombinantly expressed in Escherichia coli. An effective purification protocol was established. The purified protein, which had a purity of >95%, was identified by SDS-PAGE and MALDI-TOF MS. The protein was crystallized using the vapour-diffusion method in hanging-drop mode with PEG 3350 as the primary precipitant. X-ray diffraction data were collected to 2.1 Å resolution. Preliminary X-ray analysis indicated that the crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 52.25, b = 63.29, c = 131.81 Å.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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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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Bacterial Proteins / metabolism
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Buffers
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Crystallization
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Diffusion
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / chemistry
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Escherichia coli / metabolism
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Humans
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Hydrogen-Ion Concentration
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Phosphoribosylglycinamide Formyltransferase / chemistry*
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Phosphoribosylglycinamide Formyltransferase / genetics
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Phosphoribosylglycinamide Formyltransferase / isolation & purification
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Phosphoribosylglycinamide Formyltransferase / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Streptococcus mutans / enzymology*
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X-Ray Diffraction
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X-Rays
Substances
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Bacterial Proteins
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Buffers
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Recombinant Proteins
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Phosphoribosylglycinamide Formyltransferase