Journal
JOURNAL OF SYNCHROTRON RADIATION
Volume 18, Issue -, Pages 16-19Publisher
WILEY-BLACKWELL PUBLISHING, INC
DOI: 10.1107/S090904951003445X
Keywords
semi-solid agarose gels; top-seeded solution growth; large-scale hanging-drop method; X-ray crystallography; neutron crystallography
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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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