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- W2064667263 abstract "Crystallization can be used as a purification method for proteins. Lysozyme was chosen as a model substance. Changing crystallization conditions will lead as shown to different lysozyme crystal morphologies with different properties. Beside others, lysozyme crystals can show a Tetragonal, High Temperature and Low Temperature Orthorhombic crystal morphology. Experiments such as conductivity measurements, pH tests, chloride detection tests, experiments using methylene blue as a dye and dissolution experiments were carried out to investigate the composition of the lysozyme crystals. It is proven that lysozyme crystals are made up of the initial buffer solution components: lysozyme (the protein), water which is part of the crystal lattice, salt ions which are attached to the protein molecule and voids filled with the buffer solution containing the crystallization agent (e.g. salt). Interesting dissolution behaviours of the lysozyme crystals were observed which are not described so far elsewhere (© 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim)" @default.
- W2064667263 created "2016-06-24" @default.
- W2064667263 creator A5055284231 @default.
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- W2064667263 date "2011-06-07" @default.
- W2064667263 modified "2023-09-25" @default.
- W2064667263 title "A more clear insight of the lysozyme crystal composition" @default.
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- W2064667263 doi "https://doi.org/10.1002/crat.201100134" @default.
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