Molecules 2010, 15(2), 793-803; doi:10.3390/molecules15020793
Communication

The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H2O Mixtures and a Novel Approach to Protein Crystallization

Received: 16 December 2009; in revised form: 2 February 2010 / Accepted: 4 February 2010 / Published: 4 February 2010
(This article belongs to the Special Issue Ionic Liquids)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
Keywords: protic ionic liquids; protein crystallization; solubility and protein stability
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MDPI and ACS Style

Byrne, N.; Angell, C.A. The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H2O Mixtures and a Novel Approach to Protein Crystallization. Molecules 2010, 15, 793-803.

AMA Style

Byrne N, Angell CA. The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H2O Mixtures and a Novel Approach to Protein Crystallization. Molecules. 2010; 15(2):793-803.

Chicago/Turabian Style

Byrne, Nolene; Angell, C. Austen. 2010. "The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H2O Mixtures and a Novel Approach to Protein Crystallization." Molecules 15, no. 2: 793-803.

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