Crystallization of cyclosporin A in lyotropic reverse hexagonal liquid crystals

Dima Libster; Abraham Aserin; Idit Amar-Yuli; Tehila Mishraki; Yael Domovich-Eisenberg; Oded Livnah; Nissim Garti

doi:10.1039/c001263g

Crystallization of cyclosporin A in lyotropic reverse hexagonal liquid crystals

Dima Libster, Abraham Aserin, Idit Amar-Yuli, Tehila Mishraki, Yael Domovich-Eisenberg, Oded Livnah, Nissim Garti^*

^*Corresponding author for this work

Department of Biological Chemistry

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

In this communication we demonstrate for the first time that lyotropic reverse hexagonal mesophase can serve as a crystallization medium for a hydrophobic peptide, resulting in high quality single crystals suitable for crystallographic analysis. The obtained crystals of cyclosporin A enabled excellent X-ray data collection, diffracting to a resolution limit of 1.0 . Current findings open a new perspective in the field of crystallization of biological macromolecules in lyotropic mesophases.

Original language	English
Pages (from-to)	2034-2036
Number of pages	3
Journal	CrystEngComm
Volume	12
Issue number	7
DOIs	https://doi.org/10.1039/c001263g
State	Published - Jul 2010

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abstract = "In this communication we demonstrate for the first time that lyotropic reverse hexagonal mesophase can serve as a crystallization medium for a hydrophobic peptide, resulting in high quality single crystals suitable for crystallographic analysis. The obtained crystals of cyclosporin A enabled excellent X-ray data collection, diffracting to a resolution limit of 1.0 . Current findings open a new perspective in the field of crystallization of biological macromolecules in lyotropic mesophases.",

author = "Dima Libster and Abraham Aserin and Idit Amar-Yuli and Tehila Mishraki and Yael Domovich-Eisenberg and Oded Livnah and Nissim Garti",

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AU - Aserin, Abraham

AU - Amar-Yuli, Idit

AU - Mishraki, Tehila

AU - Domovich-Eisenberg, Yael

AU - Livnah, Oded

AU - Garti, Nissim

PY - 2010/7

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AB - In this communication we demonstrate for the first time that lyotropic reverse hexagonal mesophase can serve as a crystallization medium for a hydrophobic peptide, resulting in high quality single crystals suitable for crystallographic analysis. The obtained crystals of cyclosporin A enabled excellent X-ray data collection, diffracting to a resolution limit of 1.0 . Current findings open a new perspective in the field of crystallization of biological macromolecules in lyotropic mesophases.

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Crystallization of cyclosporin A in lyotropic reverse hexagonal liquid crystals

Abstract

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