Open AccessExpression, crystallization and preliminary X‐ray analysis of the phosphoribosylglycinamide formyltransferase from Streptococcus mutans
Author(s) -
Zhai Fangli,
Liu Xiaojuan,
Ruan Jing,
Li Jing,
Liu Zhenlong,
Hu Yulin,
Li Shentao
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110053170
Subject(s) - streptococcus mutans , escherichia coli , crystallization , resolution (logic) , chemistry , crystallography , peg ratio , microbiology and biotechnology , chromatography , biology , bacteria , biochemistry , gene , genetics , organic chemistry , finance , artificial intelligence , computer science , economics
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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 52.25, b = 63.29, c = 131.81 Å.