On the crystallization of proteins
Identifieur interne : 000821 ( Istex/Curation ); précédent : 000820; suivant : 000822On the crystallization of proteins
Auteurs : Z. Kam [États-Unis, Israël] ; H. B. Shore [États-Unis] ; G. Feher [États-Unis]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1978.
English descriptors
- Teeft :
- Academic press, Aggregate, Aggregation, Aggregation process, Amorphous, Amorphous aggregates, Amorphous precipitates, Amorphous precipitation, Chem, Compact structure, Critical size, Crystal, Crystal growth, Crystal surface, Crystalline aggregates, Crystallization, Different lysozyme concentrations, Different ratios, Differential equation, Diffusion coefficient, Diffusion coefficients, Equilibrium constants, Error hypothesis, Experimental conditions, Experimental results, External conditions, Foreign bodies, Homogeneous nucleation, Kztal ktmor, Large crystals, Large difference, Large number, Large ratio, Larger aggregates, Lowest energy, Lysozyme, Lysozyme concentration, Lysozyme crystals, Marcel dekker, Mild supersaturation, Model system, Molecular level, Monomer, Monomer concentration, Next section, Nucleation, Nucleation process, Numerical values, Ohara reid, Original size, Phys, Power spectrum, Previous section, Protein concentration, Protein concentration profile, Protein crystals, Protein molecules, Quartz slides, Quasielastic light, Salt concentration, Several orders, Simple model, Size distribution, Slow growth, Small aggregates, Small number, Solid line, Solubility limit, Spectral distribution, Spectrum analyzer, Surface area, Surface term, Systematic approach, Terminal size, Theoretical model, Time dependence, Time development, Time interval, True equilibrium, Ultraviolet light, Unit concentration, Usable crystals, Visible crystals.
Abstract
Abstract: We report on theoretical and experimental work aimed at a systematic approach to the crystallization of proteins. Successful crystallization depends on the competition between the growth rates for compact three-dimensional structures and long-chain structures leading to an amorphous precipitate. Quasi-elastic light scattering was used to monitor the size and shape distribution of small aggregates in a model system (lysozyme) during the pre-nucleation stage. With the aid of a simple model, the line-width of the scattered light was used to predict whether crystals or an amorphous precipitate would result. Once visible crystals appeared, the lysozyme concentration near the crystal surface was monitored and the kinetic parameters for growth obtained. A peculiar self-limiting phenomenon causes crystals to stop growing after a certain size has been reached. When these terminal size crystals were cleaved, growth occurred at the surface until the original size was approximately restored.
Url:
DOI: 10.1016/0022-2836(78)90206-1
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Shore</name><affiliation wicri:level="1"><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics, University of California San Diego, La Jolla, Calif. 92093</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>Also Department of Physics, San Diego State University, San Diego, Calif. 92182, U.S.A.</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Also Department of Physics, San Diego State University, San Diego, Calif. 92182</wicri:regionArea></affiliation></author><author><name sortKey="Feher, G" sort="Feher, G" uniqKey="Feher G" first="G." last="Feher">G. Feher</name><affiliation wicri:level="1"><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics, University of California San Diego, La Jolla, Calif. 92093</wicri:regionArea></affiliation><affiliation><mods:affiliation>To whom reprint requests should be sent.</mods:affiliation><wicri:noCountry code="no comma">To whom reprint requests should be sent.</wicri:noCountry></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:FCED8FEEA170BB6F262CB2621F3A6C23102FE2A5</idno><date when="1978" year="1978">1978</date><idno type="doi">10.1016/0022-2836(78)90206-1</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-5WBGBF6B-J/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000821</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000821</idno><idno type="wicri:Area/Istex/Curation">000821</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">On the crystallization of proteins</title><author><name sortKey="Kam, Z" sort="Kam, Z" uniqKey="Kam Z" first="Z." last="Kam">Z. 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Shore</name><affiliation wicri:level="1"><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics, University of California San Diego, La Jolla, Calif. 92093</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>Also Department of Physics, San Diego State University, San Diego, Calif. 92182, U.S.A.</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Also Department of Physics, San Diego State University, San Diego, Calif. 92182</wicri:regionArea></affiliation></author><author><name sortKey="Feher, G" sort="Feher, G" uniqKey="Feher G" first="G." last="Feher">G. Feher</name><affiliation wicri:level="1"><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physics, University of California San Diego, La Jolla, Calif. 92093</wicri:regionArea></affiliation><affiliation><mods:affiliation>To whom reprint requests should be sent.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="ISSN">0022-2836</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1978">1978</date><biblScope unit="volume">123</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="539">539</biblScope><biblScope unit="page" to="555">555</biblScope></imprint><idno type="ISSN">0022-2836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-2836</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Aggregate</term><term>Aggregation</term><term>Aggregation process</term><term>Amorphous</term><term>Amorphous aggregates</term><term>Amorphous precipitates</term><term>Amorphous precipitation</term><term>Chem</term><term>Compact structure</term><term>Critical size</term><term>Crystal</term><term>Crystal growth</term><term>Crystal surface</term><term>Crystalline aggregates</term><term>Crystallization</term><term>Different lysozyme concentrations</term><term>Different ratios</term><term>Differential equation</term><term>Diffusion coefficient</term><term>Diffusion coefficients</term><term>Equilibrium constants</term><term>Error hypothesis</term><term>Experimental conditions</term><term>Experimental results</term><term>External conditions</term><term>Foreign bodies</term><term>Homogeneous nucleation</term><term>Kztal ktmor</term><term>Large crystals</term><term>Large difference</term><term>Large number</term><term>Large ratio</term><term>Larger aggregates</term><term>Lowest energy</term><term>Lysozyme</term><term>Lysozyme concentration</term><term>Lysozyme crystals</term><term>Marcel dekker</term><term>Mild supersaturation</term><term>Model system</term><term>Molecular level</term><term>Monomer</term><term>Monomer concentration</term><term>Next section</term><term>Nucleation</term><term>Nucleation process</term><term>Numerical values</term><term>Ohara reid</term><term>Original size</term><term>Phys</term><term>Power spectrum</term><term>Previous section</term><term>Protein concentration</term><term>Protein concentration profile</term><term>Protein crystals</term><term>Protein molecules</term><term>Quartz slides</term><term>Quasielastic light</term><term>Salt concentration</term><term>Several orders</term><term>Simple model</term><term>Size distribution</term><term>Slow growth</term><term>Small aggregates</term><term>Small number</term><term>Solid line</term><term>Solubility limit</term><term>Spectral distribution</term><term>Spectrum analyzer</term><term>Surface area</term><term>Surface term</term><term>Systematic approach</term><term>Terminal size</term><term>Theoretical model</term><term>Time dependence</term><term>Time development</term><term>Time interval</term><term>True equilibrium</term><term>Ultraviolet light</term><term>Unit concentration</term><term>Usable crystals</term><term>Visible crystals</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: We report on theoretical and experimental work aimed at a systematic approach to the crystallization of proteins. Successful crystallization depends on the competition between the growth rates for compact three-dimensional structures and long-chain structures leading to an amorphous precipitate. Quasi-elastic light scattering was used to monitor the size and shape distribution of small aggregates in a model system (lysozyme) during the pre-nucleation stage. With the aid of a simple model, the line-width of the scattered light was used to predict whether crystals or an amorphous precipitate would result. Once visible crystals appeared, the lysozyme concentration near the crystal surface was monitored and the kinetic parameters for growth obtained. A peculiar self-limiting phenomenon causes crystals to stop growing after a certain size has been reached. When these terminal size crystals were cleaved, growth occurred at the surface until the original size was approximately restored.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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