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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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| Główni autorzy: | , , , , |
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| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
International Union of Crystallography
2007
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| Hasła przedmiotowe: | |
| Dostęp online: | 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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