CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE RECEPTOR-BINDING DOMAIN OF HUMAN AND BOVINE ALPHA(2)-MACROGLOBULIN

Citation
K. Dolmer et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE RECEPTOR-BINDING DOMAIN OF HUMAN AND BOVINE ALPHA(2)-MACROGLOBULIN, FEBS letters, 372(1), 1995, pp. 93-95
Citations number
32
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
372
Issue
1
Year of publication
1995
Pages
93 - 95
Database
ISI
SICI code
0014-5793(1995)372:1<93:CAPAOT>2.0.ZU;2-E
Abstract
The receptor-binding domains (RBDs) of human and bovine alpha(2)-macro globulin (alpha(2)M) have been isolated after limited proteolysis of m ethylamine-treated alpha(2)M with papain. Single crystals of the RBDs have been grown by vapour diffusion. Crystals of human RED are very th in plates unsuited for data collection. However, crystals of RED from bovine alpha(2)M give diffraction patterns suitable for X-ray analysis , and a complete dataset with a maximum resolution of 2.3 Angstrom has been collected with synchrotron radiation at cryogenic temperature, T he crystals belong to spacegroup P3(1)21 or P3(2)21 with cell paramete rs a = b = 106.8 Angstrom, c = 72.2 Angstrom.