title: Preliminary crystallographic analyses of the N-terminal lobe of recombinant human serum transferrin.
abstract: The N-terminal lobe of recombinant human serum transferrin (residues 1 to 337) has been crystallized in a form suitable for high-resolution three-dimensional X-ray crystallographic analyses. Crystals are of the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 44.9 A, b = 57.0 A and c = 135.9 A, and diffract to beyond 2 A resolution. Further studies show that isomorphous crystals of specifically designed mutants of this protein can also be grown. Structural studies of both recombinant and mutant protein forms will provide a basis for understanding the mechanism by which human serum transferrin functions.
authors.affiliation: Department of Biochemistry, University of British Columbia, Vancouver, Canada.
authors.forename: Y
authors.initials: Y
authors.lastname: Wang
authors.forename: J
authors.initials: J
authors.lastname: Chen
authors.forename: Y
authors.initials: Y
authors.lastname: Luo
authors.forename: W D
authors.initials: WD
authors.lastname: Funk
authors.forename: A B
authors.initials: AB
authors.lastname: Mason
authors.forename: R C
authors.initials: RC
authors.lastname: Woodworth
authors.forename: R T
authors.initials: RT
authors.lastname: MacGillivray
authors.forename: G D
authors.initials: GD
authors.lastname: Brayer
mesh_terms: D003460:Crystallization; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry; D014168:Transferrin / Q000737:chemistry*
chemical_list: D011994:Recombinant Proteins; D014168:Transferrin