Approach for growth of high-quality and large protein crystals
Three crystallization methods for growing large high-quality protein crystals, i.e. crystallization in the presence of a semi-solid agarose gel, top-seeded solution growth (TSSG) and a large-scale hanging-drop method, have previously been presented. In this study the effectiveness of crystallization...
Veröffentlicht in: | Journal of synchrotron radiation. - 1994. - 18(2011), 1 vom: 28. Jan., Seite 16-9 |
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1. Verfasser: | |
Weitere Verfasser: | , , , , , , , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2011
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Zugriff auf das übergeordnete Werk: | Journal of synchrotron radiation |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Gels Proteins Solutions Sepharose 9012-36-6 Muramidase EC 3.2.1.17 |
Zusammenfassung: | Three crystallization methods for growing large high-quality protein crystals, i.e. crystallization in the presence of a semi-solid agarose gel, top-seeded solution growth (TSSG) and a large-scale hanging-drop method, have previously been presented. In this study the effectiveness of crystallization in the presence of a semi-solid agarose gel has been further evaluated by crystallizing additional proteins in the presence of 2.0% (w/v) agarose gel, resulting in complete gelification with high mechanical strength. In TSSG the seed crystals are hung by a seed holder protruding from the top of the growth vessel to prevent polycrystallization. In the large-scale hanging-drop method, a cut pipette tip was used to maintain large-scale droplets consisting of protein-precipitant solution. Here a novel crystallization method that combines TSSG and the large-scale hanging-drop method is reported. A large and single crystal of lysozyme was obtained by this method |
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Beschreibung: | Date Completed 04.04.2011 Date Revised 20.10.2021 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1600-5775 |
DOI: | 10.1107/S090904951003445X |