Expression, purification and preliminary crystallographic analysis of O-acetylhomoserine sulfhydrylase from Mycobacterium tuberculosis.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 67(Pt 8): 959-63, 2011 Aug 01.
Article
em En
| MEDLINE
| ID: mdl-21821905
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 2.1â
Å.
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1
Base de dados:
MEDLINE
Assunto principal:
Carbono-Oxigênio Liases
/
Mycobacterium tuberculosis
Limite:
Humans
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article