Thermostable exoshells fold and stabilize recombinant proteins
Improving recombinant protein expression and stabilization remains a significant challenge. Here, the authors engineer Archaeoglobus fulgidus ferritin as a thermostable exoshell to provide steric accommodation and charge complementation for recombinant proteins, which can improve yields by 100 fold.
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2017-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-017-01585-2 |