Crystallization and preliminary X-ray diffraction analysis of P30, the transmembrane domain of pertactin, an autotransporter from Bordetella pertussis.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 63(Pt 7): 593-5, 2007 Jul 01.
Article
em En
| MEDLINE
| ID: mdl-17620719
ABSTRACT
P30, the 32 kDa transmembrane C-terminal domain of pertactin from Bordetella pertussis, is supposed to form a beta-barrel inserted into the outer membrane for the translocation of the passenger domain. P30 was cloned and expressed in inclusion bodies in Escherichia coli. After refolding and purification, the protein was crystallized using the sitting-drop vapour-diffusion method at 292 K. The crystals diffract to a resolution limit of 3.5 A using synchrotron radiation and belong to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 123.27, c = 134.43 A.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas da Membrana Bacteriana Externa
/
Bordetella pertussis
/
Fatores de Virulência de Bordetella
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Reino Unido