Crystallization and molecular replacement solution of human heparin binding protein

被引：4

作者：

Iversen, LF ^{[1
]}

Kastrup, JS ^{[1
]}

Larsen, IK ^{[1
]}

Bjorn, SE ^{[1
]}

Rasmussen, PB ^{[1
]}

Wiberg, FC ^{[1
]}

Flodgaard, HJ ^{[1
]}

机构：

[1] NOVO NORDISK AS,DK-2880 BAGSVAERD,DENMARK

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1996年 / 52卷

关键词：

D O I：

10.1107/S0907444996010086

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom. Ethanol was used as precipitant and glycerol as additive. A full data set has been collected to 3.1 Angstrom and diffraction was observed to at least 2.3 Angstrom 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.

引用

页码：1222 / 1223

页数：2

共 12 条

[1]

[Anonymous], ACTA CRYSTALLOGR D

[2] HUMAN-LEUKOCYTE AND PORCINE PANCREATIC ELASTASE - X-RAY CRYSTAL-STRUCTURES, MECHANISM, SUBSTRATE-SPECIFICITY, AND MECHANISM-BASED INHIBITORS [J].