Publikationsdatum:
2015-03-20
Beschreibung:
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 inVibrio cholerae. To obtain structural insights into the periplasmic haem-binding protein HutB fromV. 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 1.6 Mammonium sulfate as a precipitant at pH 7.0. X-ray diffraction data were collected to 2.4 Å resolution on the RRCAT PX-BL-21 beamline at the Indus-2 synchrotron, Indore, India. The crystals belonged to space groupP43212, with unit-cell parametersa=b= 62.88,c= 135.8 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 withPhaserconfirmed the presence of a monomer in the asymmetric unit.
Digitale ISSN:
2053-230X
Thema:
Biologie
,
Chemie und Pharmazie
,
Geologie und Paläontologie
,
Physik
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