title: Crystallization and preliminary X-ray analysis of Gc, the vitamin D-binding protein in serum.
abstract: The vitamin D-binding protein, Gc, was purified from human serum and crystallized using the hanging-drop method. The best crystals were grown from 28% polyethylene glycol 400 in 50 mM-sodium acetate at pH 4.8. These crystals diffract to 3.4 A and the observed diffraction is consistent with orthorhombic space groups P4(1) and P4(3). The unit cell parameters were determined to be a = b = 135.5 A and c = 75.6 A.
authors.affiliation: Department of Chemistry, Princeton University, NJ 08544.
authors.forename: N J
authors.initials: NJ
authors.lastname: Vogelaar
authors.forename: U
authors.initials: U
authors.lastname: Lindberg
authors.forename: C E
authors.initials: CE
authors.lastname: Schutt
mesh_terms: D002852:Chromatography, Ion Exchange; D003460:Crystallization; D006801:Humans; D011487:Protein Conformation; D014809:Vitamin D-Binding Protein / Q000097:blood* / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D014809:Vitamin D-Binding Protein