title: Crystallization and X-ray investigation of vitamin D-binding protein from human serum. Identification of the crystal content.
abstract: Vitamin D-binding protein (DBP), a multifunctional, highly polymorphic glycoprotein responsible for the transport of vitamin D and for sequestering extracellular actin, was isolated from human serum and crystallized using vapour diffusion methods. The crystals were grown from 7.5% v/v polyethylene glycol 400 and 0.1 M acetate buffer at pH 4.6. These crystals show diffraction patterns consistent with the tetragonal space groups P4(1) and P4(3) with unit cell dimensions a = b = 135.5(4) A and c = 75.9(4) A. They diffract to 2.3 A. Using polyacrylamide gel electrophoresis it was shown that according to their electrophoretic mobility the O-glycosylated isoforms, with a terminal sialic acid residue, are absent in the crystals.
authors.affiliation: Laboratorium voor Analytische Chemie en Medicinale Fysicochemie, Faculteit Farmaceutische Wetenschappen, Katholieke Universiteit Leuven, Belgium.
authors.forename: C C
authors.initials: CC
authors.lastname: Verboven
authors.forename: H L
authors.initials: HL
authors.lastname: De Bondt
authors.forename: C
authors.initials: C
authors.lastname: De Ranter
authors.forename: R
authors.initials: R
authors.lastname: Bouillon
authors.forename: H
authors.initials: H
authors.lastname: Van Baelen
mesh_terms: D003460:Crystallization; D006801:Humans; D014809:Vitamin D-Binding Protein / Q000097:blood / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D014809:Vitamin D-Binding Protein