Abstract
We report on the solubility of hen lysozyme (HEWL) in aqueous ethylammonium nitrate (EAN) as a function of water content. We find the solubility behavior to be complex, exhibiting both a maximum (400 mg/mL) at very high EAN content) and a minimum at intermediate EAN content. We exploit this solubility profile in a novel approach to generating crystals of hydrophilic proteins, based on rehydration of a high concentration protein solution. We describe the production of crystals of X-ray diffraction quality. Two related ionic liquid solvent systems, with the same solubility profiles but different effective pH characteristics, are identified for future evaluation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 793-803 |
| Number of pages | 11 |
| Journal | Molecules |
| Volume | 15 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 2010 |
Keywords
- Protein crystallization
- Protic ionic liquids
- Solubility and protein stability
ASJC Scopus subject areas
- Analytical Chemistry
- Chemistry (miscellaneous)
- Molecular Medicine
- Pharmaceutical Science
- Drug Discovery
- Physical and Theoretical Chemistry
- Organic Chemistry