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Cleaved thioredoxin fusion protein enables the crystallization of poorly soluble ERα in complex with synthetic ligands

The ligand-binding domain (LBD) of human oestrogen receptor α 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 a...

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Bibliografski detalji
Glavni autori: Cura, Vincent, Gangloff, Monique, Eiler, Sylvia, Moras, Dino, Ruff, Marc
Format: Artigo
Jezik:Inglês
Izdano: International Union of Crystallography 2007
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2373989/
https://ncbi.nlm.nih.gov/pubmed/18097104
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309107066444
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