Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of the GyrA subunit of DNA gyrase from Staphylococcus aureus strain Mu50.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 67(Pt 2): 277-9, 2011 Feb 01.
Article
en En
| MEDLINE
| ID: mdl-21301105
ABSTRACT
DNA gyrase is a type II topoisomerase that is essential for chromosome segregation and cell division owing to its ability to modify the topological form of bacterial DNA. In this study, the C-terminal domain of the GyrA subunit of DNA gyrase from Staphylococcus aureus Mu50 strain was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.80â
Å resolution using a synchrotron-radiation source. The crystal belonged to space group P2(1), with unit-cell parameters a = 37.28, b = 80.19, c = 50.22â
Å, ß = 110.64°. The asymmetric unit contained one molecule, with a corresponding V(M) of 2.02â
Å(3)â
Da(-1) and a solvent content of 39.2%.
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1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Staphylococcus aureus
/
Proteínas Bacterianas
/
Girasa de ADN
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2011
Tipo del documento:
Article