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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt 7):723-6. doi: 10.1107/S174430910902291X. Epub 2009 Jun 27.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Heme-Binding Proteins
  • Hemeproteins / chemistry*
  • Humans
  • Pregnancy Proteins / chemistry*

Substances

  • Carrier Proteins
  • HEBP1 protein, human
  • HEBP2 protein, human
  • Heme-Binding Proteins
  • Hemeproteins
  • Pregnancy Proteins