Crystallization and molecular replacement solution of human heparin binding protein

The highly glycosylated protein, human heparin binding protein, has been crystallized in the primitive orthorhombic space group P2₁2₁2₁ with cell dimensions a = 39.0, b = 66.2 and c = 101.4 Å. Ethanol was used as precipitant and glycerol as additive. A full data set has been collected to 3.1 Å and diffraction was observed to at least 2.3 Å. A molecular replacement solution using human neutrophile elastase as a search model was obtained, showing one molecule per asymmetric unit. The crystal packing showed no bad contacts and the R factor was 44.8% after ten cycles of rigid-body refinement.