Crystallization and preliminary X-ray analysis of recombinant human transforming growth factor beta 2.
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.
Schlunegger
M P
MP
Department of Biotechnology, Ciba-Geigy Ltd., Basel, Switzerland.
Cerletti
N
N
Cox
D A
DA
McMaster
G K
GK
Schmitz
A
A
Grütter
M G
MG
D016475:3T3 Cells; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D011994:Recombinant Proteins / Q000378:metabolism; D016212:Transforming Growth Factor beta / Q000378:metabolism*; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D016212:Transforming Growth Factor beta