title: Preliminary crystallographic studies on human complement pro-factor D.
abstract: The recombinant zymogen of the human complement protein factor D has been crystallized. Crystals were grown by vapor diffusion using polyethylene glycol 6000 as precipitant. Two crystal forms obtained at pH 5.4 belong to space group P2(1). The crystals grow to dimensions of 0.6 mm x 0.3 mm x 0.3 mm in three days, are stable in the X-ray beam, and diffract to 2.4 A.
authors.affiliation: Center for Macromolecular Crystallography, University of Alabama at Birmingham 25294.
authors.forename: S V
authors.initials: SV
authors.lastname: Narayana
authors.forename: Y
authors.initials: Y
authors.lastname: Yamauchi
authors.forename: K J
authors.initials: KJ
authors.lastname: Macon
authors.forename: D
authors.initials: D
authors.lastname: Moore
authors.forename: L J
authors.initials: LJ
authors.lastname: DeLucas
authors.forename: J E
authors.initials: JE
authors.lastname: Volanakis
mesh_terms: D000595:Amino Acid Sequence; D011416:Complement Factor D / Q000648:ultrastructure*; D018360:Crystallography, X-Ray; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000648:ultrastructure; D006801:Humans; D008969:Molecular Sequence Data; D011994:Recombinant Proteins
chemical_list: D004792:Enzyme Precursors; D011994:Recombinant Proteins; C493488:CFD protein, human; D011416:Complement Factor D