Format

Send to

Choose Destination
FEBS Lett. 1992 May 25;303(1):91-3.

Crystallization and preliminary X-ray analysis of recombinant human transforming growth factor beta 2.

Author information

1
Department of Biotechnology, Ciba-Geigy Ltd., Basel, Switzerland.

Abstract

Recombinant human transforming growth factor beta 2 (TGF-beta 2) was cloned and expressed in E. coli. The protein was isolated from inclusion bodies, renatured and purified to a single component as judged by reversed-phase HPLC. The recombinant TGF-beta 2 was shown to have a biological activity equal to that of native TGF-beta 2 in a fibroblast migration assay. Pure, active recombinant TGF-beta 2 has been crystallized from polyethylene glycol 400. The trigonal crystals of spacegroup P3(1)21 or P3(2)21 have unit cell dimensions of a=b=60.6 A, c=75.2 A and diffract beyond 2.0 A.

PMID:
1592122
DOI:
10.1016/0014-5793(92)80484-x
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center