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.
