Structural determination of lipid-bound human blood coagulation factor IX

S. Stoylova, E. Gray, T. W. Barrowcliffe, G. Kemball-Cook, A. Holzenburg

Research output: Contribution to journalArticle

8 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)175-178
Number of pages4
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1383
Issue number2
DOIs
StatePublished - Apr 2 1998

Keywords

  • Human blood coagulation factor IX
  • Lipid-protein interaction
  • Macromolecular organisation
  • Membrane binding
  • Transmission electron microscopy and crystallography
  • Two-dimensional crystallization

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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