Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 63(Pt 4): 353-5, 2007 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-17401215
ABSTRACT
Phosphoglucose isomerase is a ubiquitous enzyme that catalyzes the isomerization of D-glucopyranose-6-phosphate to D-fructofuranose-6-phosphate. The present investigation reports the expression, purification, crystallization and preliminary crystallographic studies of the phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv, which shares 46% sequence identity with that of its human host. The recombinant protein, which was prepared using an Escherichia coli expression system, was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.8 A and belonged to the orthorhombic space group I2(1)2(1)2(1), with unit-cell parameters a = 109.0, b = 119.8, c = 138.9 A.
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1
Coleções:
01-internacional
Temas:
Geral
Base de dados:
MEDLINE
Assunto principal:
Glucose-6-Fosfato Isomerase
/
Mycobacterium tuberculosis
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Índia