Journal
MOLECULES
Volume 15, Issue 2, Pages 793-803Publisher
MDPI
DOI: 10.3390/molecules15020793
Keywords
protic ionic liquids; protein crystallization; solubility and protein stability
Funding
- NSF [CHE0404714]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0909120] Funding Source: National Science Foundation
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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.
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