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Updated: Jul 19, 2026
Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Preparation, crystallization and preliminary X-ray analysis of the methionine synthase (MetE) from Streptococcus
Tian Min Fu1, Xiao Yan Zhang, Lan Fen Li
1National Laboratory of Protein Engineering and Plant Genetic Engineering, Peking University, Beijing 100871, People's Republic of China.
Abstract:
The Streptococcus mutans metE gene encodes methionine synthase (MetE), which catalyzes the direct transfer of a methyl group from methyltetrahydrofolate to homocysteine in the last step of methionine synthesis. metE was cloned into pET28a and the gene product was expressed at high levels in the Escherichia coli strain BL21 (DE3). MetE was purified to homogeneity using Ni(2+)-chelating chromatography followed by size-exclusion chromatography. Crystals of the protein were obtained by the hanging-drop vapour-diffusion method and diffracted to 2.2 A resolution. The crystal belongs to space group P2(1), with unit-cell parameters a = 52.85, b = 99.48, c = 77.88 A, beta = 94.55 degrees .
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