Crystallization and preliminary X‐ray analysis of recombinant human transforming growth factor β2

FEBS Letters

Schmitz, Albert¹  Schlunegger, Michael P.¹  Grütter, Markus G.¹  Cox, David A.¹  Cerletti, Nico¹  McMaster, Gary K.¹ 

[1] Department of Biotechnology, Pharmaceuticals Division, Ciba-Geigy Lid., CH-4002 Basel, Switzerland

关键词: Transforming growth factor β2;    Protein crystallization;    Crystallography;   

DOI  :  10.1016/0014-5793(92)80484-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recombinant human transforming growth factor β2 (TGF-β2) 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-β2 was shown to have a biological activity equal to that of native TGF-β2 in a fibroblast migration assay. Pure, active recombinant TGF-β2 has been crystallized from polyethylene glycol 400. The trigonal crystals of spacegroup P3₁21 or P3₂21 have unit cell dimensions of a=b=60.6 Å, c=75.2 Å and diffract beyond 2.0 Å.

【 授权许可】

Unknown