On the crystallization of proteins
Identifieur interne : 000821 ( Istex/Corpus ); précédent : 000820; suivant : 000822On the crystallization of proteins
Auteurs : Z. Kam ; H. B. Shore ; G. FeherSource :
- 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
Links to Exploration step
ISTEX:FCED8FEEA170BB6F262CB2621F3A6C23102FE2A5Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>On the crystallization of proteins</title><author><name sortKey="Kam, Z" sort="Kam, Z" uniqKey="Kam Z" first="Z." last="Kam">Z. Kam</name><affiliation><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation></affiliation><affiliation><mods:affiliation>† Present address: Polymer Department, The Weizmann Institute of Science, Rehovot, Israel.</mods:affiliation></affiliation></author><author><name sortKey="Shore, H B" sort="Shore, H B" uniqKey="Shore H" first="H. B." last="Shore">H. B. Shore</name><affiliation><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation></affiliation><affiliation><mods:affiliation>Also Department of Physics, San Diego State University, San Diego, Calif. 92182, U.S.A.</mods:affiliation></affiliation></author><author><name sortKey="Feher, G" sort="Feher, G" uniqKey="Feher G" first="G." last="Feher">G. Feher</name><affiliation><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation></affiliation><affiliation><mods:affiliation>To whom reprint requests should be sent.</mods:affiliation></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></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. Kam</name><affiliation><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation></affiliation><affiliation><mods:affiliation>† Present address: Polymer Department, The Weizmann Institute of Science, Rehovot, Israel.</mods:affiliation></affiliation></author><author><name sortKey="Shore, H B" sort="Shore, H B" uniqKey="Shore H" first="H. B." last="Shore">H. B. Shore</name><affiliation><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation></affiliation><affiliation><mods:affiliation>Also Department of Physics, San Diego State University, San Diego, Calif. 92182, U.S.A.</mods:affiliation></affiliation></author><author><name sortKey="Feher, G" sort="Feher, G" uniqKey="Feher G" first="G." last="Feher">G. Feher</name><affiliation><mods:affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</mods:affiliation></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><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>lysozyme</json:string><json:string>nucleation</json:string><json:string>phys</json:string><json:string>chem</json:string><json:string>size distribution</json:string><json:string>lysozyme concentration</json:string><json:string>aggregation</json:string><json:string>nucleation process</json:string><json:string>academic press</json:string><json:string>terminal size</json:string><json:string>monomer</json:string><json:string>aggregation process</json:string><json:string>crystal growth</json:string><json:string>power spectrum</json:string><json:string>small aggregates</json:string><json:string>protein concentration</json:string><json:string>crystallization</json:string><json:string>time dependence</json:string><json:string>protein crystals</json:string><json:string>marcel dekker</json:string><json:string>large number</json:string><json:string>previous section</json:string><json:string>different lysozyme concentrations</json:string><json:string>experimental results</json:string><json:string>solubility limit</json:string><json:string>critical size</json:string><json:string>amorphous aggregates</json:string><json:string>next section</json:string><json:string>theoretical model</json:string><json:string>amorphous precipitation</json:string><json:string>aggregate</json:string><json:string>different ratios</json:string><json:string>compact structure</json:string><json:string>surface term</json:string><json:string>crystal surface</json:string><json:string>surface area</json:string><json:string>visible crystals</json:string><json:string>lowest energy</json:string><json:string>external conditions</json:string><json:string>ohara reid</json:string><json:string>unit concentration</json:string><json:string>systematic approach</json:string><json:string>equilibrium constants</json:string><json:string>lysozyme crystals</json:string><json:string>large ratio</json:string><json:string>crystalline aggregates</json:string><json:string>large crystals</json:string><json:string>quasielastic light</json:string><json:string>simple model</json:string><json:string>time development</json:string><json:string>usable crystals</json:string><json:string>solid line</json:string><json:string>true equilibrium</json:string><json:string>monomer concentration</json:string><json:string>mild supersaturation</json:string><json:string>molecular level</json:string><json:string>foreign bodies</json:string><json:string>experimental conditions</json:string><json:string>salt concentration</json:string><json:string>kztal ktmor</json:string><json:string>protein molecules</json:string><json:string>homogeneous nucleation</json:string><json:string>spectral distribution</json:string><json:string>diffusion coefficient</json:string><json:string>model system</json:string><json:string>diffusion coefficients</json:string><json:string>larger aggregates</json:string><json:string>slow growth</json:string><json:string>spectrum analyzer</json:string><json:string>small number</json:string><json:string>amorphous precipitates</json:string><json:string>large difference</json:string><json:string>protein concentration profile</json:string><json:string>quartz slides</json:string><json:string>ultraviolet light</json:string><json:string>differential equation</json:string><json:string>time interval</json:string><json:string>original size</json:string><json:string>several orders</json:string><json:string>error hypothesis</json:string><json:string>numerical values</json:string><json:string>crystal</json:string><json:string>amorphous</json:string></teeft></keywords><author><json:item><name>Z. Kam</name><affiliations><json:string>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</json:string><json:string>† Present address: Polymer Department, The Weizmann Institute of Science, Rehovot, Israel.</json:string></affiliations></json:item><json:item><name>H.B. Shore</name><affiliations><json:string>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</json:string><json:string>Also Department of Physics, San Diego State University, San Diego, Calif. 92182, U.S.A.</json:string></affiliations></json:item><json:item><name>G. Feher</name><affiliations><json:string>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</json:string><json:string>To whom reprint requests should be sent.</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-5WBGBF6B-J</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><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.</abstract><qualityIndicators><score>8.728</score><pdfWordCount>5045</pdfWordCount><pdfCharCount>36812</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>17</pdfPageCount><pdfPageSize>468 x 684 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>144</abstractWordCount><abstractCharCount>1004</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>On the crystallization of proteins</title><pmid><json:string>691056</json:string></pmid><pii><json:string>0022-2836(78)90206-1</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>part C</title><language><json:string>unknown</json:string></language></serie><host><title>Journal of Molecular Biology</title><language><json:string>unknown</json:string></language><publicationDate>1978</publicationDate><issn><json:string>0022-2836</json:string></issn><pii><json:string>S0022-2836(00)X1024-8</json:string></pii><volume>123</volume><issue>4</issue><pages><first>539</first><last>555</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>10s</json:string><json:string>1855</json:string><json:string>1978</json:string></date><geogName></geogName><orgName><json:string>National Science Foundation</json:string><json:string>Also Department of Physics, San Diego Statp Univrrqity, San Diego, Calif</json:string><json:string>Sigma Corp.</json:string><json:string>Weizmann Institute of Science, Rehovot, Israel</json:string><json:string>National Institutes of Health</json:string><json:string>Academic Press Inc.</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>N. H. Xuong</json:string><json:string>H. Reiss</json:string><json:string>B. H. Zimm</json:string><json:string>Gibbs</json:string><json:string>Volmer</json:string><json:string>M. Weissman</json:string><json:string>Crystal Growth</json:string><json:string>J. Kraut</json:string><json:string>La Jolla</json:string></persName><placeName><json:string>GAj</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Zeldovich, 1942</json:string><json:string>Humphreys-Owen, 1949</json:string><json:string>Andres, 1969</json:string><json:string>Blundell & Johnson, 1976</json:string><json:string>Dubin, 1972</json:string><json:string>Dunning, 1969</json:string><json:string>Chu, 1974</json:string><json:string>Dubin et al., 1973</json:string><json:string>Volmer & Wcber, 1926</json:string><json:string>I’olmer $ Floods 1934; Volmer, 1939</json:string><json:string>Ohara & Reid, 1973</json:string><json:string>Sultan, 1952</json:string><json:string>Joll&s & Berthou, 1972</json:string><json:string>Blundell & *Johnson, 1976</json:string><json:string>Reisler & Eisenberg, 1971</json:string><json:string>Castellan, 1964</json:string><json:string>Matthews, 1976</json:string><json:string>Xuong, 1969</json:string><json:string>Benedek, 1969</json:string><json:string>illderton & Fevold, 1946</json:string><json:string>Cummins & Rwinney, 1970</json:string><json:string>Orgel, 1963</json:string><json:string>Steinrauf, 1959</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-5WBGBF6B-J</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1978</publicationDate><copyrightDate>1978</copyrightDate><doi><json:string>10.1016/0022-2836(78)90206-1</json:string></doi><id>FCED8FEEA170BB6F262CB2621F3A6C23102FE2A5</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-5WBGBF6B-J/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-5WBGBF6B-J/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-5WBGBF6B-J/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">On the crystallization of proteins</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1978</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note>The work was supported by grants from the National Institutes of Health (GM 13191) and the National Science Foundation (DMR 74-24361).</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">On the crystallization of proteins</title><author xml:id="author-0000"><persName><forename type="first">Z.</forename><surname>Kam</surname></persName><affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</affiliation><affiliation>† Present address: Polymer Department, The Weizmann Institute of Science, Rehovot, Israel.</affiliation></author><author xml:id="author-0001"><persName><forename type="first">H.B.</forename><surname>Shore</surname></persName><affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</affiliation><affiliation>Also Department of Physics, San Diego State University, San Diego, Calif. 92182, U.S.A.</affiliation></author><author xml:id="author-0002"><persName><forename type="first">G.</forename><surname>Feher</surname></persName><affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</affiliation><affiliation>To whom reprint requests should be sent.</affiliation></author><idno type="istex">FCED8FEEA170BB6F262CB2621F3A6C23102FE2A5</idno><idno type="ark">ark:/67375/6H6-5WBGBF6B-J</idno><idno type="DOI">10.1016/0022-2836(78)90206-1</idno><idno type="PII">0022-2836(78)90206-1</idno></analytic><monogr><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="pISSN">0022-2836</idno><idno type="PII">S0022-2836(00)X1024-8</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="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></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1978</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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.</p></abstract></profileDesc><revisionDesc><change when="1978">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-5WBGBF6B-J/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>YJMBI</jid><aid>78902061</aid><ce:pii>0022-2836(78)90206-1</ce:pii><ce:doi>10.1016/0022-2836(78)90206-1</ce:doi><ce:copyright type="unknown" year="1978"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>The work was supported by grants from the National Institutes of Health (GM 13191) and the National Science Foundation (DMR 74-24361).</ce:note-para></ce:article-footnote><ce:title>On the crystallization of proteins</ce:title><ce:author-group><ce:author><ce:given-name>Z.</ce:given-name><ce:surname>Kam</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>H.B.</ce:given-name><ce:surname>Shore</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>G.</ce:given-name><ce:surname>Feher</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="COR1"><ce:sup>§</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>‡</ce:label><ce:textfn>Also Department of Physics, San Diego State University, San Diego, Calif. 92182, U.S.A.</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>§</ce:label><ce:text>To whom reprint requests should be sent.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>†</ce:label><ce:note-para>Present address: Polymer Department, The Weizmann Institute of Science, Rehovot, Israel.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="13" month="12" year="1977"></ce:date-received><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>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 <ce:italic>model system</ce:italic> (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.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>On the crystallization of proteins</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>On the crystallization of proteins</title></titleInfo><name type="personal"><namePart type="given">Z.</namePart><namePart type="family">Kam</namePart><affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</affiliation><affiliation>† Present address: Polymer Department, The Weizmann Institute of Science, Rehovot, Israel.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.B.</namePart><namePart type="family">Shore</namePart><affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</affiliation><affiliation>Also Department of Physics, San Diego State University, San Diego, Calif. 92182, U.S.A.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Feher</namePart><affiliation>Department of Physics, University of California San Diego, La Jolla, Calif. 92093, U.S.A.</affiliation><affiliation>To whom reprint requests should be sent.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1978</dateIssued><copyrightDate encoding="w3cdtf">1978</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract 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.</abstract><note>The work was supported by grants from the National Institutes of Health (GM 13191) and the National Science Foundation (DMR 74-24361).</note><relatedItem type="host"><titleInfo><title>Journal of Molecular Biology</title></titleInfo><titleInfo type="abbreviated"><title>YJMBI</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1978</dateIssued></originInfo><identifier type="ISSN">0022-2836</identifier><identifier type="PII">S0022-2836(00)X1024-8</identifier><part><date>1978</date><detail type="volume"><number>123</number><caption>vol.</caption></detail><detail type="issue"><number>4</number><caption>no.</caption></detail><extent unit="issue-pages"><start>505</start><end>726</end></extent><extent unit="pages"><start>539</start><end>555</end></extent></part></relatedItem><identifier type="istex">FCED8FEEA170BB6F262CB2621F3A6C23102FE2A5</identifier><identifier type="ark">ark:/67375/6H6-5WBGBF6B-J</identifier><identifier type="DOI">10.1016/0022-2836(78)90206-1</identifier><identifier type="PII">0022-2836(78)90206-1</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-5WBGBF6B-J/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000821 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 000821 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:FCED8FEEA170BB6F262CB2621F3A6C23102FE2A5
|texte= On the crystallization of proteins
}}
| This area was generated with Dilib version V0.6.33. |  |