Preparation, crystallization and preliminary X-ray analysis of the methionine synthase (MetE) from Streptococcus mutans
- National Laboratory of Protein Engineering and Plant Genetic Engineering, Peking University, Beijing 100871 (China)
Methionine synthase (MetE) from S. mutans was expressed, purified and crystallized. Diffraction data have been collected to 2.2 Å resolution. 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{sup 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 Å resolution. The crystal belongs to space group P2{sub 1}, with unit-cell parameters a = 52.85, b = 99.48, c = 77.88 Å, β = 94.55°.
- OSTI ID:
- 22356370
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 10; Other Information: PMCID: PMC2225190; PMID: 17012790; PUBLISHER-ID: ll5078; OAI: oai:pubmedcentral.nih.gov:2225190; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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