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 P2(1)2(1)2(1) with cell dimensions a = 39.0, b = 66.2 and c = 101.4 A. Ethanol was used as precipitant and glycerol as additive. A full data set has been collected to 3.1 A and diffraction was observed to at least 2.3 A. 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.
Iversen
L F
LF
Department of Medicinal Chemistry, Royal Danish School of Pharmacy, Copenhagen, Denmark. lars@medchem.dfh.dk
Kastrup
J S
JS
Larsen
I K
IK
Bjørn
S E
SE
Rasmussen
P B
PB
Wiberg
F C
FC
Flodgaard
H J
HJ