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Preliminary structural characterization of human SOUL, a haem-binding protein.


ABSTRACT: Human SOUL (hSOUL) is a 23 kDa haem-binding protein that was first identified as the PP(23) protein isolated from human full-term placentas. Here, the overexpression, purification and crystallization of hSOUL are reported. The crystals belonged to space group P6(4)22, with unit-cell parameters a = b = 145, c = 60 A and one protein molecule in the asymmetric unit. X-ray diffraction data were collected to 3.5 A resolution at the ESRF. A preliminary model of the three-dimensional structure of hSOUL was obtained by molecular replacement using the structures of murine p22HBP (PDB codes 2gov and 2hva), obtained by solution NMR, as search models.

SUBMITTER: Freire F 

PROVIDER: S-EPMC2705645 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature

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Preliminary structural characterization of human SOUL, a haem-binding protein.

Freire Filipe F   Romão Maria João MJ   Macedo Anjos L AL   Aveiro Susana S SS   Goodfellow Brian J BJ   Carvalho Ana Luísa AL  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090627 Pt 7


Human SOUL (hSOUL) is a 23 kDa haem-binding protein that was first identified as the PP(23) protein isolated from human full-term placentas. Here, the overexpression, purification and crystallization of hSOUL are reported. The crystals belonged to space group P6(4)22, with unit-cell parameters a = b = 145, c = 60 A and one protein molecule in the asymmetric unit. X-ray diffraction data were collected to 3.5 A resolution at the ESRF. A preliminary model of the three-dimensional structure of hSOUL  ...[more]

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