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Article in English | MEDLINE | ID: mdl-21301108

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 Šresolution. 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.


Subject(s)
Bacterial Proteins/chemistry , Phosphoribosylglycinamide Formyltransferase/chemistry , Streptococcus mutans/enzymology , Amino Acid Sequence , Bacterial Proteins/genetics , Bacterial Proteins/isolation & purification , Bacterial Proteins/metabolism , Buffers , Crystallization , Diffusion , Electrophoresis, Polyacrylamide Gel , Escherichia coli/chemistry , Escherichia coli/metabolism , Humans , Hydrogen-Ion Concentration , Phosphoribosylglycinamide Formyltransferase/genetics , Phosphoribosylglycinamide Formyltransferase/isolation & purification , Phosphoribosylglycinamide Formyltransferase/metabolism , Recombinant Proteins/chemistry , Recombinant Proteins/isolation & purification , Recombinant Proteins/metabolism , Sequence Homology, Amino Acid , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , X-Ray Diffraction , X-Rays
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