Linked Data Explorerhttp://worldcat.org/entity/work/id/1862910406
Crystallization of proteins by dynamic control of supersaturation
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http://schema.org/about
- http://id.worldcat.org/fast/1127829
- http://id.worldcat.org/fast/819505
- http://id.worldcat.org/fast/798293
- http://id.worldcat.org/fast/1181820
- http://experiment.worldcat.org/entity/work/data/1862910406#Topic/proteins_analysis
- http://id.loc.gov/authorities/subjects/sh85107668
- http://id.loc.gov/authorities/subjects/sh85148730
- http://id.loc.gov/authorities/subjects/sh85001359
- http://id.worldcat.org/fast/1079714
- http://experiment.worldcat.org/entity/work/data/1862910406#Topic/x_ray_crystallography
- http://id.loc.gov/authorities/subjects/sh85125953
- http://id.worldcat.org/fast/1204155
- http://id.loc.gov/authorities/subjects/sh85008968
http://schema.org/description
- ""The growth of protein crystals in known to be the limiting factor in the determination of the three-dimensional structures of most proteins. It is expected that the kinetics of supersaturation, which is directly related to solvent evaporation, will affect protein crystal growth and nucleation and accordingly determine the quality, number, size and morphology of the crystals. With a technique that controls the evaporation of solvent from a protein solution with N[subscript]2 (g) it is possible to determine the effect of different evaporation profiles on hen egg white lysozyme crystals. Hen egg white lysozyme was chosen as the model protein because it crystallizes easily and has solubility data available for most salt, pH and temperature ranges. Commercially available lysozyme was further purified by a number of methods. Crystals grown with the purified lysozyme and with the unpurified lysozyme in citrate buffer were different shapes but were found to be of the same symmetry space group by precession photos. Differences were seen in the lysozyme crystals grown using different evaporation rates. At three of the four initial conditions for lysozyme crystal growth longer evaporation times yielded better crystals. The evaporation times required to see a change in the appearance of the crystals was much longer than expected. The number of rates studied so far represent only a small fraction of the ones now available with the gas evaporation device. The technique also provides for control of both solution pH and temperature which are related to the solubilities of proteins." --P. xv."
http://schema.org/name
- "Crystallization of proteins by dynamic control of supersaturation"@en
- "Crystallization of proteins by dynamic control of supersaturation"