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 language | English (US) |
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Pages (from-to) | 175-178 |
Number of pages | 4 |
Journal | Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology |
Volume | 1383 |
Issue number | 2 |
DOIs | |
State | Published - Apr 2 1998 |
Externally published | Yes |
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