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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

†,*  and
Department of Chemistry and Biochemistry, Arizona State University, Tempe 85287, AZ, USA Current address: Centre for Materials and Fibre Innovation, Institute for Technology Research & Innovation, Deakin University, Geelong, Victoria 3217, Australia
* Author to whom correspondence should be addressed.
Received: 16 December 2009 / Revised: 2 February 2010 / Accepted: 4 February 2010 / Published: 4 February 2010
(This article belongs to the Special Issue Ionic Liquids)
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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 protic ionic liquids; protein crystallization; solubility and protein stability
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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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.

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