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

被引：5

作者：

DOLMER, K

JENNER, LB

JACOBSEN, L

ANDERSEN, GR

KOCH, TJ

THIRUP, S

SOTTRUPJENSEN, L

NYBORG, J

机构：

[1] AARHUS UNIV,DEPT CHEM,DK-8000 AARHUS C,DENMARK

[2] AARHUS UNIV,DEPT BIOL MOLEC,DK-8000 AARHUS C,DENMARK

[3] AARHUS UNIV,DEPT MED BIOCHEM,DK-8000 AARHUS C,DENMARK

来源：

FEBS LETTERS | 1995年 / 372卷 / 01期

关键词：

ALPHA-MACROGLOBULIN; RECEPTOR-BINDING; CRYSTALLIZATION;

D O I：

10.1016/0014-5793(95)00960-H

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The receptor-binding domains (RBDs) of human and bovine alpha(2)-macroglobulin (alpha(2)M) have been isolated after limited proteolysis of methylamine-treated alpha(2)M with papain. Single crystals of the RBDs have been grown by vapour diffusion. Crystals of human RED are very thin 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, The crystals belong to spacegroup P3(1)21 or P3(2)21 with cell parameters a = b = 106.8 Angstrom, c = 72.2 Angstrom.

引用

页码：93 / 95

页数：3

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[3]

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