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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...
में बचाया:
| मुख्य लेखकों: | , , , , |
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| स्वरूप: | Artigo |
| भाषा: | Inglês |
| प्रकाशित: |
International Union of Crystallography
2007
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| विषय: | |
| ऑनलाइन पहुंच: | 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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