The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H(2)O Mixtures and a Novel Approach to Protein Crystallization

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 solubili...

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Detalles Bibliográficos
Autores principales: Byrne, Nolene, Angell, C. Austen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International 2010
Materias:
Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6257119/
https://www.ncbi.nlm.nih.gov/pubmed/20335946
http://dx.doi.org/10.3390/molecules15020793
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author Byrne, Nolene
Angell, C. Austen
author_facet Byrne, Nolene
Angell, C. Austen
author_sort Byrne, Nolene
collection PubMed
description 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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spelling pubmed-62571192018-12-03 The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H(2)O Mixtures and a Novel Approach to Protein Crystallization Byrne, Nolene Angell, C. Austen Molecules Communication 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. Molecular Diversity Preservation International 2010-02-04 /pmc/articles/PMC6257119/ /pubmed/20335946 http://dx.doi.org/10.3390/molecules15020793 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Communication
Byrne, Nolene
Angell, C. Austen
The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H(2)O Mixtures and a Novel Approach to Protein Crystallization
title The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H(2)O Mixtures and a Novel Approach to Protein Crystallization
title_full The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H(2)O Mixtures and a Novel Approach to Protein Crystallization
title_fullStr The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H(2)O Mixtures and a Novel Approach to Protein Crystallization
title_full_unstemmed The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H(2)O Mixtures and a Novel Approach to Protein Crystallization
title_short The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H(2)O Mixtures and a Novel Approach to Protein Crystallization
title_sort solubility of hen lysozyme in ethylammonium nitrate/h(2)o mixtures and a novel approach to protein crystallization
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6257119/
https://www.ncbi.nlm.nih.gov/pubmed/20335946
http://dx.doi.org/10.3390/molecules15020793
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