S. Karlsen et al., ATOMIC-RESOLUTION STRUCTURE OF HUMAN HBP CAP37/AZUROCIDIN/, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 598-609
Citations number
33
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
Crystals of human heparin binding protein (HBP) diffract to 1.1 Angstr
om when flash-frozen at 120 K. The atomic resolution structure has bee
n refined anisotropically using SHELXL96. The final model of HBP consi
sts of 221 amino-acid residues of 225 possible, three glycosylation un
its, one chloride ion, 15 precipitant ethanol molecules and 323 water
molecules. The structure is refined to a final crystallographic R fact
or of 15.9% and R-free(5%) of 18.9% using all data. A putative protein
kinase C activation site has been identified, involving residues 113-
120. The structure is compared to the previously determined 2.3 Angstr
om resolution structure of HBP.