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Expression, purification and preliminary crystallographic analysis of O-acetylhomoserine sulfhydrylase from Mycobacterium tuberculosis.

ABSTRACT: The gene product of the open reading frame Rv3340 from Mycobacterium tuberculosis is annotated as encoding a probable O-acetylhomoserine (OAH) sulfhydrylase (MetC), an enzyme that catalyzes the last step in the biosynthesis of methionine, which is an essential amino acid in bacteria and plants. Following overexpression in Escherichia coli, the M. tuberculosis MetC enzyme was purified and crystallized using the hanging-drop vapor-diffusion method. Native diffraction data were collected from crystals belonging to space group P2(1) and were processed to a resolution of 2.1?Å.

SUBMITTER: Yin J

PROVIDER: S-EPMC3151138 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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Expression, purification and preliminary crystallographic analysis of O-acetylhomoserine sulfhydrylase from Mycobacterium tuberculosis.

Yin Jiang J Garen Craig R CR Bateman Katherine K Yu Minmin M Lyon Emily Z Alipio EZ Habel Jeff J Kim Heungbok H Hung Li-wei LW Kim Chang-Yub CY James Michael N G MN

Acta crystallographica. Section F, Structural biology and crystallization communications 20110727 Pt 8

The gene product of the open reading frame Rv3340 from Mycobacterium tuberculosis is annotated as encoding a probable O-acetylhomoserine (OAH) sulfhydrylase (MetC), an enzyme that catalyzes the last step in the biosynthesis of methionine, which is an essential amino acid in bacteria and plants. Following overexpression in Escherichia coli, the M. tuberculosis MetC enzyme was purified and crystallized using the hanging-drop vapor-diffusion method. Native diffraction data were collected from cryst ...[more]

PMID: 21821905

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