Article
Cleaved thioredoxin fusion protein enables the crystallization of poorly soluble ERalpha in complex with synthetic ligands.
Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Jan 2008
Cura Vincent, Gangloff Monique, Eiler Sylvia, Moras Dino, Ruff Marc
Abstract excerpt
The ligand-binding domain (LBD) of human oestrogen receptor alpha was produced in Escherichia coli as a cleavable thioredoxin (Trx) fusion in order to improve solubility. Crystallization trials with either cleaved and purified LBD or with the purified fusion protein both failed to produce crystals. In another attempt, Trx was not removed from the LBD after endoproteolytic cleavage and its presence promoted...
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