title: Structural determination of lipid-bound human blood coagulation factor IX.
abstract: Human coagulation factor IX (FIX) is a serine protease which binds to a negatively charged phospholipid surface in the presence of Ca ions (Ca2+). FIX two-dimensional (2-D) crystals were obtained by the lipid layer crystallisation technique under near physiological conditions. The 2-D projection map of the protein was calculated to a resolution of 3 nm using electron crystallographic analysis. The structural organisation of membrane-bound FIX is discussed and compared with the known X-ray crystallographic data.
authors.affiliation: University of Leeds, School of Biochemistry and Molecular Biology, UK. svetla@bmb.leeds.ac.uk
authors.forename: S
authors.initials: S
authors.lastname: Stoylova
authors.forename: E
authors.initials: E
authors.lastname: Gray
authors.forename: T W
authors.initials: TW
authors.lastname: Barrowcliffe
authors.forename: G
authors.initials: G
authors.lastname: Kemball-Cook
authors.forename: A
authors.initials: A
authors.lastname: Holzenburg
mesh_terms: D001665:Binding Sites; D018360:Crystallography, X-Ray; D005164:Factor IX / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D050356:Lipid Metabolism; D011487:Protein Conformation
chemical_list: D005164:Factor IX