Purification, crystallization and preliminary X-ray analysis of the periplasmic haem-binding protein HutB from Vibrio cholerae.
Acta Crystallogr F Struct Biol Commun
; 71(Pt 4): 401-4, 2015 Apr.
Article
em En
| MEDLINE
| ID: mdl-25849499
ABSTRACT
The mechanism of haem transport across the inner membrane of pathogenic bacteria is currently insufficiently understood at the molecular level and no information is available for this process in Vibrio cholerae. To obtain structural insights into the periplasmic haem-binding protein HutB from V. cholerae (VcHutB), which is involved in haem transport through the HutBCD haem-transport system, at the atomic level, VcHutB was cloned, overexpressed and crystallized using 1.6â
M ammonium sulfate as a precipitant at pH 7.0. X-ray diffraction data were collected to 2.4â
Å resolution on the RRCAT PX-BL-21 beamline at the Indus-2 synchrotron, Indore, India. The crystals belonged to space group P43212, with unit-cell parameters a = b = 62.88, c = 135.8â
Å. Matthews coefficient calculations indicated the presence of one monomer in the asymmetric unit, with an approximate solvent content of 45.02%. Molecular-replacement calculations with Phaser confirmed the presence of a monomer in the asymmetric unit.
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MEDLINE
Assunto principal:
Vibrio cholerae
/
Proteínas de Transporte
/
Periplasma
/
Hemeproteínas
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article