Crystallisation and preliminary X‐ray analysis of the receptor‐binding domain of human and bovine α 2‐macroglobulin

FEBS Letters

Nyborg, Jens³  Jenner, Lasse B³  Sottrup-Jensen, Lars²  Koch, Trine J³  Thirup, Søren³  Dolmer, Klavs²  Jacobsen, Linda¹  Andersen, Gregers R³ 

[1] Department of Medical Biochemistry, University of Århus, DK-8000 Århus C, Denmark;Department of Molecular Biology, University of Århus, DK-8000 Århus C, Denmark;Department of Chemistry, University of Århus, DK-8000 Århus C, Denmark

关键词: α-Macroglobulin;    Receptor-binding;    Crystallization;    α 2M;    α 2- macroglobulin;    α 2M-MA;    methylamine-treated α 2-macroglobulin;    α 2MR/LRP;    α 2M receptor/low density lipoprotein receptor-related protein;    β-OGP;    1-O-n-Octyl-β-D-glucopyranoside;    Con A;    Concanavalin A;    G1cNH2;    glucosamine;    Hepes;    N-(2-hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid);    Mes;    2-(N-morpholino)ethanesulfonic acid;    NaP;    Sodium phosphate;    PEG;    Polyethylene glycol;    RBD;    Receptor-binding domain of α2M (approx. residues 13141451);    SDS-PAGE;    sodium dodecyl sulphate polyacrylamide gel electrophoresis;    Tris;    Tris(hydroxymethyl)amino-methane;   

DOI  :  10.1016/0014-5793(95)00960-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The receptor-binding domains (RBDs) of human and bovine α ₂-macroglobulin (α ₂M) have been isolated after limited proteolysis of methylamine-treated α ₂M with papain. Single crystals of the RBDs have been grown by vapour diffusion. Crystals of human RBD are very thin plates unsuited for data collection. However, crystals of RBD from bovine α ₂M give diffraction patterns suitable for X-ray analysis, and a complete dataset with a maximum resolution of 2.3 Å has been collected with synchrotron radiation at cryogenic temperature. The crystals belong to spacegroup P3₁21 or P3₂21 with cell parameters , .

【 授权许可】

Unknown