Nucleation and crystallization of globular proteins — what we know and what is missing
Identifieur interne : 000D83 ( Istex/Corpus ); précédent : 000D82; suivant : 000D84Nucleation and crystallization of globular proteins — what we know and what is missing
Auteurs : F. Rosenberger ; P. G. Vekilov ; M. Muschol ; B. R. ThomasSource :
- Journal of Crystal Growth [ 0022-0248 ] ; 1996.
English descriptors
- Teeft :
- Acid residues, Acta, Acta cryst, Aggregation, Asymmetric unit, Atomic force microscopy, Attractive forces, Attractive interactions, Authentic protein standards, Avidin, Avidin incorporation, Brookhaven protein database, Bulk solution, Bulk transport, Chem, Compositional, Compositional inhomogeneities, Convection, Convective transport, Corresponding rocking width profile, Coulomb repulsion, Crys values, Cryst, Crystal, Crystal contacts, Crystal growth, Crystal perfection, Crystal size, Crystallization, Crystallization cell, Crystallization conditions, Defect, Defect formation, Depletion zones, Diffraction resolution, Diffusive transport, Diffusivities, Dimer, Direct interactions, Dislocation, Dislocation formation, Dislocation groups, Dislocation step sources, Dlvo potentials, Dynamic data, Dynamic light, Electrostatic repulsion, Etching features, Facet, Facet edges, Fine striations, Fluctuation, Fluctuation amplitude, Full symbols, Globular, Globular proteins, Grain boundary, Growth conditions, Growth kinetics, Growth morphology, Growth rate, Growth rate fluctuations, Growth rates, Growth sector boundaries, Growth steps, Growth units, Hewl, Hewl crystal, Hewl crystallization, Hewl crystals, Hewl dimer, Hewl face, Hewl solutions, Hexamer, High supersaturations, Hydrodynamic, Hydrodynamic interaction term, Hydrodynamic interactions, Hydrophobic, Hydrophobic groups, Impurity, Impurity effects, Impurity repartitioning, Incorporation, Incorporation mechanism, Inhomogeneity, Initial lysozyme concentration, Initial solutions, Inorganic crystals, Inorganic materials, Inorganic solution growth, Inorganic systems, Interaction effects, Interfacial kinetics, Kinetics, Large impurities, Large number, Linear dependence, Local slope, Long wavelength limit, Lysozyme, Lysozyme concentration, Lysozyme molecule, Lysozyme molecules, Macromolecular crystallization community, Macromolecule, Mass density, Materials research, Mcpherson, Mole ratio, Molecular weight, Molecule, Monomer, More efforts, Normal gravity, Normal growth rate, Nucleation, Nucleation events, Numerous proteins, Other hand, Other proteins, Oxford university press, Phys, Precipitant, Protein, Protein charge, Protein concentration, Protein concentrations, Protein crystal, Protein crystallization, Protein crystals, Protein impurities, Protein interactions, Protein ions, Protein molecules, Protein solutions, Purer seikagaku solutions, Real crystal structure, Recent work, Repartitioning, Repulsion, Rosenberger, Scenario, Seikagaku, Seikagaku solution, Side chains, Sigma, Sigma solutions, Silver stain, Similar observations, Smaller crystals, Sodium acetate buffer, Solute, Solute concentration, Solute particles, Solution conditions, Space experiments, Specific antibodies, Staining techniques, Static light, Static structure factor, Step generation, Step motion, Step sources, Striation, Striation formation, Structural perfection, Structural quality, Supersaturated solutions, Supersaturation, Supersaturation conditions, Supersaturations, Surface charge, Surface nucleation, Surface separation, Synchrotron topographs, Tangential velocity, Temperature changes, Topographs, Transport conditions, Typical crystallization conditions, Undersaturated solutions, Unit cell, Unrelated proteins, Various concentrations, Various nac1 concentrations, Various supersaturations, Vekilov.
Abstract
Abstract: Recently, much progress has been made in understanding the nucleation and crystallization of globular proteins, including the formation of compositional and structural crystal defects. Insight into the interactions of (screened) protein macro-ions in solution, obtained from light scattering, small angle X-ray scattering and osmotic pressure studies, can guide the search for crystallization conditions. These studies show that the nucleation of globular proteins is governed by the same principles as that of small molecules. However, failure to account for direct and indirect (hydrodynamic) protein interactions in the solutions results in unrealistic aggregation scenarios. Microscopic studies of numerous proteins reveal that crystals grow by the attachment of growth units through the same layer-spreading mechanisms as inorganic crystals. Investigations of the growth kinetics of hen-egg-white lysozyme (HEWL) reveal non-steady behavior under steady external conditions. Long-term variations in growth rates are due to changes in step-originating dislocation groups. Fluctuations on a shorter timescale reflect the non-linear dynamics of layer growth that results from the interplay between interfacial kinetics and bulk transport. Systematic gel electrophoretic analyses suggest that most HEWL crystallization studies have been performed with material containing other proteins at percent levels. Yet, sub-percent levels of protein impurities impede growth step propagation and play a role in the formation of structural/compositional inhomogeneities. In crystal growth from highly purified HEWL solutions, however, such inhomogeneities are much weaker and form only in response to unusually large changes in growth conditions. Equally important for connecting growth conditions to crystal perfection and diffraction resolution are recent advances in structural characterization through high-resolution Bragg reflection profiling and X-ray topography.
Url:
DOI: 10.1016/0022-0248(96)00358-2
Links to Exploration step
ISTEX:01CE8274DA1904DF6B6EFC5CEFB9673F12E30B89Le document en format XML
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Rosenberger</name><affiliation><mods:affiliation>Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA</mods:affiliation></affiliation></author><author><name sortKey="Vekilov, P G" sort="Vekilov, P G" uniqKey="Vekilov P" first="P. G." last="Vekilov">P. G. Vekilov</name><affiliation><mods:affiliation>Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA</mods:affiliation></affiliation></author><author><name sortKey="Muschol, M" sort="Muschol, M" uniqKey="Muschol M" first="M." last="Muschol">M. Muschol</name><affiliation><mods:affiliation>Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA</mods:affiliation></affiliation></author><author><name sortKey="Thomas, B R" sort="Thomas, B R" uniqKey="Thomas B" first="B. R." last="Thomas">B. R. Thomas</name><affiliation><mods:affiliation>Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Crystal Growth</title><title level="j" type="abbrev">CRYS</title><idno type="ISSN">0022-0248</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">168</biblScope><biblScope unit="issue">1–4</biblScope><biblScope unit="page" from="1">1</biblScope><biblScope unit="page" to="27">27</biblScope></imprint><idno type="ISSN">0022-0248</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-0248</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acid residues</term><term>Acta</term><term>Acta cryst</term><term>Aggregation</term><term>Asymmetric unit</term><term>Atomic force microscopy</term><term>Attractive forces</term><term>Attractive interactions</term><term>Authentic protein standards</term><term>Avidin</term><term>Avidin incorporation</term><term>Brookhaven protein database</term><term>Bulk solution</term><term>Bulk transport</term><term>Chem</term><term>Compositional</term><term>Compositional inhomogeneities</term><term>Convection</term><term>Convective transport</term><term>Corresponding rocking width profile</term><term>Coulomb repulsion</term><term>Crys values</term><term>Cryst</term><term>Crystal</term><term>Crystal contacts</term><term>Crystal growth</term><term>Crystal perfection</term><term>Crystal size</term><term>Crystallization</term><term>Crystallization cell</term><term>Crystallization conditions</term><term>Defect</term><term>Defect formation</term><term>Depletion zones</term><term>Diffraction resolution</term><term>Diffusive transport</term><term>Diffusivities</term><term>Dimer</term><term>Direct interactions</term><term>Dislocation</term><term>Dislocation formation</term><term>Dislocation groups</term><term>Dislocation step sources</term><term>Dlvo potentials</term><term>Dynamic data</term><term>Dynamic light</term><term>Electrostatic repulsion</term><term>Etching features</term><term>Facet</term><term>Facet edges</term><term>Fine striations</term><term>Fluctuation</term><term>Fluctuation amplitude</term><term>Full symbols</term><term>Globular</term><term>Globular proteins</term><term>Grain boundary</term><term>Growth conditions</term><term>Growth kinetics</term><term>Growth morphology</term><term>Growth rate</term><term>Growth rate fluctuations</term><term>Growth rates</term><term>Growth sector boundaries</term><term>Growth steps</term><term>Growth units</term><term>Hewl</term><term>Hewl crystal</term><term>Hewl crystallization</term><term>Hewl crystals</term><term>Hewl dimer</term><term>Hewl face</term><term>Hewl solutions</term><term>Hexamer</term><term>High supersaturations</term><term>Hydrodynamic</term><term>Hydrodynamic interaction term</term><term>Hydrodynamic interactions</term><term>Hydrophobic</term><term>Hydrophobic groups</term><term>Impurity</term><term>Impurity effects</term><term>Impurity repartitioning</term><term>Incorporation</term><term>Incorporation mechanism</term><term>Inhomogeneity</term><term>Initial lysozyme concentration</term><term>Initial solutions</term><term>Inorganic crystals</term><term>Inorganic materials</term><term>Inorganic solution growth</term><term>Inorganic systems</term><term>Interaction effects</term><term>Interfacial kinetics</term><term>Kinetics</term><term>Large impurities</term><term>Large number</term><term>Linear dependence</term><term>Local slope</term><term>Long wavelength limit</term><term>Lysozyme</term><term>Lysozyme concentration</term><term>Lysozyme molecule</term><term>Lysozyme molecules</term><term>Macromolecular crystallization community</term><term>Macromolecule</term><term>Mass density</term><term>Materials research</term><term>Mcpherson</term><term>Mole ratio</term><term>Molecular weight</term><term>Molecule</term><term>Monomer</term><term>More efforts</term><term>Normal gravity</term><term>Normal growth rate</term><term>Nucleation</term><term>Nucleation events</term><term>Numerous proteins</term><term>Other hand</term><term>Other proteins</term><term>Oxford university press</term><term>Phys</term><term>Precipitant</term><term>Protein</term><term>Protein charge</term><term>Protein concentration</term><term>Protein concentrations</term><term>Protein crystal</term><term>Protein crystallization</term><term>Protein crystals</term><term>Protein impurities</term><term>Protein interactions</term><term>Protein ions</term><term>Protein molecules</term><term>Protein solutions</term><term>Purer seikagaku solutions</term><term>Real crystal structure</term><term>Recent work</term><term>Repartitioning</term><term>Repulsion</term><term>Rosenberger</term><term>Scenario</term><term>Seikagaku</term><term>Seikagaku solution</term><term>Side chains</term><term>Sigma</term><term>Sigma solutions</term><term>Silver stain</term><term>Similar observations</term><term>Smaller crystals</term><term>Sodium acetate buffer</term><term>Solute</term><term>Solute concentration</term><term>Solute particles</term><term>Solution conditions</term><term>Space experiments</term><term>Specific antibodies</term><term>Staining techniques</term><term>Static light</term><term>Static structure factor</term><term>Step generation</term><term>Step motion</term><term>Step sources</term><term>Striation</term><term>Striation formation</term><term>Structural perfection</term><term>Structural quality</term><term>Supersaturated solutions</term><term>Supersaturation</term><term>Supersaturation conditions</term><term>Supersaturations</term><term>Surface charge</term><term>Surface nucleation</term><term>Surface separation</term><term>Synchrotron topographs</term><term>Tangential velocity</term><term>Temperature changes</term><term>Topographs</term><term>Transport conditions</term><term>Typical crystallization conditions</term><term>Undersaturated solutions</term><term>Unit cell</term><term>Unrelated proteins</term><term>Various concentrations</term><term>Various nac1 concentrations</term><term>Various supersaturations</term><term>Vekilov</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Recently, much progress has been made in understanding the nucleation and crystallization of globular proteins, including the formation of compositional and structural crystal defects. Insight into the interactions of (screened) protein macro-ions in solution, obtained from light scattering, small angle X-ray scattering and osmotic pressure studies, can guide the search for crystallization conditions. These studies show that the nucleation of globular proteins is governed by the same principles as that of small molecules. However, failure to account for direct and indirect (hydrodynamic) protein interactions in the solutions results in unrealistic aggregation scenarios. Microscopic studies of numerous proteins reveal that crystals grow by the attachment of growth units through the same layer-spreading mechanisms as inorganic crystals. Investigations of the growth kinetics of hen-egg-white lysozyme (HEWL) reveal non-steady behavior under steady external conditions. Long-term variations in growth rates are due to changes in step-originating dislocation groups. Fluctuations on a shorter timescale reflect the non-linear dynamics of layer growth that results from the interplay between interfacial kinetics and bulk transport. Systematic gel electrophoretic analyses suggest that most HEWL crystallization studies have been performed with material containing other proteins at percent levels. Yet, sub-percent levels of protein impurities impede growth step propagation and play a role in the formation of structural/compositional inhomogeneities. In crystal growth from highly purified HEWL solutions, however, such inhomogeneities are much weaker and form only in response to unusually large changes in growth conditions. Equally important for connecting growth conditions to crystal perfection and diffraction resolution are recent advances in structural characterization through high-resolution Bragg reflection profiling and X-ray topography.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>crystal growth</json:string><json:string>hewl</json:string><json:string>nucleation</json:string><json:string>kinetics</json:string><json:string>rosenberger</json:string><json:string>lysozyme</json:string><json:string>supersaturation</json:string><json:string>fluctuation</json:string><json:string>dimer</json:string><json:string>solute</json:string><json:string>seikagaku</json:string><json:string>striation</json:string><json:string>dislocation</json:string><json:string>precipitant</json:string><json:string>acta cryst</json:string><json:string>cryst</json:string><json:string>acta</json:string><json:string>vekilov</json:string><json:string>impurity</json:string><json:string>protein crystallization</json:string><json:string>dynamic light</json:string><json:string>hydrodynamic</json:string><json:string>repartitioning</json:string><json:string>inhomogeneity</json:string><json:string>crystallization</json:string><json:string>phys</json:string><json:string>protein impurities</json:string><json:string>protein crystals</json:string><json:string>crystal size</json:string><json:string>diffusivities</json:string><json:string>sigma</json:string><json:string>avidin</json:string><json:string>macromolecule</json:string><json:string>globular</json:string><json:string>chem</json:string><json:string>supersaturations</json:string><json:string>hexamer</json:string><json:string>growth sector boundaries</json:string><json:string>topographs</json:string><json:string>growth kinetics</json:string><json:string>crystallization conditions</json:string><json:string>other hand</json:string><json:string>growth units</json:string><json:string>temperature changes</json:string><json:string>protein concentration</json:string><json:string>lysozyme concentration</json:string><json:string>defect formation</json:string><json:string>bulk transport</json:string><json:string>normal growth rate</json:string><json:string>hewl solutions</json:string><json:string>dislocation step sources</json:string><json:string>crystal</json:string><json:string>facet</json:string><json:string>repulsion</json:string><json:string>oxford university press</json:string><json:string>authentic protein standards</json:string><json:string>compositional inhomogeneities</json:string><json:string>large impurities</json:string><json:string>sigma solutions</json:string><json:string>seikagaku solution</json:string><json:string>tangential velocity</json:string><json:string>growth rate</json:string><json:string>striation formation</json:string><json:string>diffraction resolution</json:string><json:string>protein molecules</json:string><json:string>other proteins</json:string><json:string>hydrodynamic interactions</json:string><json:string>protein solutions</json:string><json:string>compositional</json:string><json:string>aggregation</json:string><json:string>scenario</json:string><json:string>protein</json:string><json:string>interaction effects</json:string><json:string>full symbols</json:string><json:string>static structure factor</json:string><json:string>protein concentrations</json:string><json:string>fine striations</json:string><json:string>lysozyme molecules</json:string><json:string>asymmetric unit</json:string><json:string>brookhaven protein database</json:string><json:string>inorganic systems</json:string><json:string>globular proteins</json:string><json:string>hewl dimer</json:string><json:string>surface separation</json:string><json:string>hewl crystals</json:string><json:string>bulk solution</json:string><json:string>initial solutions</json:string><json:string>high supersaturations</json:string><json:string>structural perfection</json:string><json:string>convective transport</json:string><json:string>solute particles</json:string><json:string>hewl crystal</json:string><json:string>transport conditions</json:string><json:string>crystal perfection</json:string><json:string>growth morphology</json:string><json:string>inorganic solution growth</json:string><json:string>coulomb repulsion</json:string><json:string>side chains</json:string><json:string>solution conditions</json:string><json:string>local slope</json:string><json:string>growth rates</json:string><json:string>defect</json:string><json:string>monomer</json:string><json:string>hydrophobic</json:string><json:string>similar observations</json:string><json:string>supersaturated solutions</json:string><json:string>undersaturated solutions</json:string><json:string>nucleation events</json:string><json:string>attractive interactions</json:string><json:string>unrelated proteins</json:string><json:string>recent work</json:string><json:string>impurity effects</json:string><json:string>materials research</json:string><json:string>crystal contacts</json:string><json:string>electrostatic repulsion</json:string><json:string>solute concentration</json:string><json:string>staining techniques</json:string><json:string>silver stain</json:string><json:string>specific antibodies</json:string><json:string>various concentrations</json:string><json:string>sodium acetate buffer</json:string><json:string>dynamic data</json:string><json:string>hydrodynamic interaction term</json:string><json:string>impurity repartitioning</json:string><json:string>static light</json:string><json:string>protein charge</json:string><json:string>attractive forces</json:string><json:string>inorganic materials</json:string><json:string>various nac1 concentrations</json:string><json:string>typical crystallization conditions</json:string><json:string>crys values</json:string><json:string>purer seikagaku solutions</json:string><json:string>avidin incorporation</json:string><json:string>hewl crystallization</json:string><json:string>long wavelength limit</json:string><json:string>space experiments</json:string><json:string>depletion zones</json:string><json:string>protein interactions</json:string><json:string>large number</json:string><json:string>mass density</json:string><json:string>supersaturation conditions</json:string><json:string>crystallization cell</json:string><json:string>normal gravity</json:string><json:string>protein crystal</json:string><json:string>dlvo potentials</json:string><json:string>diffusive transport</json:string><json:string>unit cell</json:string><json:string>initial lysozyme concentration</json:string><json:string>molecular weight</json:string><json:string>linear dependence</json:string><json:string>dislocation formation</json:string><json:string>hewl face</json:string><json:string>protein ions</json:string><json:string>interfacial kinetics</json:string><json:string>direct interactions</json:string><json:string>various supersaturations</json:string><json:string>smaller crystals</json:string><json:string>surface nucleation</json:string><json:string>facet edges</json:string><json:string>surface charge</json:string><json:string>acid residues</json:string><json:string>step generation</json:string><json:string>step sources</json:string><json:string>hydrophobic groups</json:string><json:string>atomic force microscopy</json:string><json:string>growth steps</json:string><json:string>step motion</json:string><json:string>inorganic crystals</json:string><json:string>macromolecular crystallization community</json:string><json:string>fluctuation amplitude</json:string><json:string>growth rate fluctuations</json:string><json:string>structural quality</json:string><json:string>incorporation mechanism</json:string><json:string>numerous proteins</json:string><json:string>etching features</json:string><json:string>grain boundary</json:string><json:string>real crystal structure</json:string><json:string>growth conditions</json:string><json:string>corresponding rocking width profile</json:string><json:string>synchrotron topographs</json:string><json:string>more efforts</json:string><json:string>dislocation groups</json:string><json:string>lysozyme molecule</json:string><json:string>mole ratio</json:string><json:string>mcpherson</json:string><json:string>convection</json:string><json:string>incorporation</json:string><json:string>molecule</json:string></teeft></keywords><author><json:item><name>F. Rosenberger</name><affiliations><json:string>Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA</json:string></affiliations></json:item><json:item><name>P.G. Vekilov</name><affiliations><json:string>Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA</json:string></affiliations></json:item><json:item><name>M. Muschol</name><affiliations><json:string>Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA</json:string></affiliations></json:item><json:item><name>B.R. Thomas</name><affiliations><json:string>Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Section I. Keynote paper</value></json:item></subject><arkIstex>ark:/67375/6H6-D6FN0XNC-B</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Recently, much progress has been made in understanding the nucleation and crystallization of globular proteins, including the formation of compositional and structural crystal defects. Insight into the interactions of (screened) protein macro-ions in solution, obtained from light scattering, small angle X-ray scattering and osmotic pressure studies, can guide the search for crystallization conditions. These studies show that the nucleation of globular proteins is governed by the same principles as that of small molecules. However, failure to account for direct and indirect (hydrodynamic) protein interactions in the solutions results in unrealistic aggregation scenarios. Microscopic studies of numerous proteins reveal that crystals grow by the attachment of growth units through the same layer-spreading mechanisms as inorganic crystals. Investigations of the growth kinetics of hen-egg-white lysozyme (HEWL) reveal non-steady behavior under steady external conditions. Long-term variations in growth rates are due to changes in step-originating dislocation groups. Fluctuations on a shorter timescale reflect the non-linear dynamics of layer growth that results from the interplay between interfacial kinetics and bulk transport. Systematic gel electrophoretic analyses suggest that most HEWL crystallization studies have been performed with material containing other proteins at percent levels. Yet, sub-percent levels of protein impurities impede growth step propagation and play a role in the formation of structural/compositional inhomogeneities. In crystal growth from highly purified HEWL solutions, however, such inhomogeneities are much weaker and form only in response to unusually large changes in growth conditions. Equally important for connecting growth conditions to crystal perfection and diffraction resolution are recent advances in structural characterization through high-resolution Bragg reflection profiling and X-ray topography.</abstract><qualityIndicators><score>10</score><pdfWordCount>12611</pdfWordCount><pdfCharCount>79060</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>27</pdfPageCount><pdfPageSize>540 x 756 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>261</abstractWordCount><abstractCharCount>1970</abstractCharCount><keywordCount>1</keywordCount></qualityIndicators><title>Nucleation and crystallization of globular proteins — what we know and what is missing</title><pii><json:string>0022-0248(96)00358-2</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Journal of Crystal Growth</title><language><json:string>unknown</json:string></language><publicationDate>1996</publicationDate><issn><json:string>0022-0248</json:string></issn><pii><json:string>S0022-0248(00)X0013-9</json:string></pii><volume>168</volume><issue>1–4</issue><pages><first>1</first><last>27</last></pages><genre><json:string>journal</json:string></genre><conference><json:item><name>Crystallization of Biological Macromolecules, Hiroshima, Japan 19951112 19951117</name></json:item></conference><editor><json:item><name>K. Miki</name></json:item><json:item><name>M. Ataka</name></json:item><json:item><name>K. Fukuyama</name></json:item><json:item><name>Y. Higuchi</name></json:item><json:item><name>T. Miyashita</name></json:item></editor></host><namedEntities><unitex><date><json:string>19951112</json:string><json:string>1996</json:string></date><geogName><json:string>Ill</json:string></geogName><orgName><json:string>National Science Foundation</json:string><json:string>University of Alabama</json:string><json:string>Materials Research, University of Alabama</json:string><json:string>National Aeronautics and Space Administration</json:string></orgName><orgName_funder><json:string>National Aeronautics and Space Administration</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>L. Carver</json:string><json:string>H. Lin</json:string><json:string>T. Miyashita</json:string><json:string>Y. Higuchi</json:string><json:string>R. Gieg</json:string><json:string>Pattern</json:string><json:string>A.A. Chernov</json:string><json:string>A. Crystals</json:string><json:string>The</json:string><json:string>J.N. Sherwood</json:string><json:string>V. Stojanoff</json:string><json:string>P.G. Vekilov</json:string><json:string>Crystal Growth</json:string><json:string>M. Ataka</json:string><json:string>H. Komatsu</json:string><json:string>W.W. Wilson</json:string><json:string>M. Ri</json:string><json:string>Materials Research</json:string><json:string>K. Fukuyama</json:string><json:string>F. Rosenberger</json:string></persName><placeName><json:string>Huntsville</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[72]</json:string><json:string>[4]</json:string><json:string>[ 122]</json:string><json:string>[45]</json:string><json:string>[102]</json:string><json:string>[121]</json:string><json:string>[84-86]</json:string><json:string>[15,16]</json:string><json:string>[39,40]</json:string><json:string>[6]</json:string><json:string>[71]</json:string><json:string>[ 103-105]</json:string><json:string>[2,3]</json:string><json:string>[107]</json:string><json:string>[100,101]</json:string><json:string>[77]</json:string><json:string>[42,43]</json:string><json:string>[6,41]</json:string><json:string>[8]</json:string><json:string>[115]</json:string><json:string>[26-29]</json:string><json:string>[47,48]</json:string><json:string>[92]</json:string><json:string>[123]</json:string><json:string>[1]</json:string><json:string>[94,108]</json:string><json:string>[87]</json:string><json:string>[53-56]</json:string><json:string>[49]</json:string><json:string>[3]</json:string><json:string>[101]</json:string><json:string>[120]</json:string><json:string>[13,14]</json:string><json:string>[117]</json:string><json:string>[80-83]</json:string><json:string>[75]</json:string><json:string>F. 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Miki</persName></editor><editor xml:id="book-author-0001"><persName>M. Ataka</persName></editor><editor xml:id="book-author-0002"><persName>K. Fukuyama</persName></editor><editor xml:id="book-author-0003"><persName>Y. Higuchi</persName></editor><editor xml:id="book-author-0004"><persName>T. Miyashita</persName></editor><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996"></date><biblScope unit="volume">168</biblScope><biblScope unit="issue">1–4</biblScope><biblScope unit="page" from="1">1</biblScope><biblScope unit="page" to="27">27</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1996</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Recently, much progress has been made in understanding the nucleation and crystallization of globular proteins, including the formation of compositional and structural crystal defects. Insight into the interactions of (screened) protein macro-ions in solution, obtained from light scattering, small angle X-ray scattering and osmotic pressure studies, can guide the search for crystallization conditions. These studies show that the nucleation of globular proteins is governed by the same principles as that of small molecules. However, failure to account for direct and indirect (hydrodynamic) protein interactions in the solutions results in unrealistic aggregation scenarios. Microscopic studies of numerous proteins reveal that crystals grow by the attachment of growth units through the same layer-spreading mechanisms as inorganic crystals. Investigations of the growth kinetics of hen-egg-white lysozyme (HEWL) reveal non-steady behavior under steady external conditions. Long-term variations in growth rates are due to changes in step-originating dislocation groups. Fluctuations on a shorter timescale reflect the non-linear dynamics of layer growth that results from the interplay between interfacial kinetics and bulk transport. Systematic gel electrophoretic analyses suggest that most HEWL crystallization studies have been performed with material containing other proteins at percent levels. Yet, sub-percent levels of protein impurities impede growth step propagation and play a role in the formation of structural/compositional inhomogeneities. In crystal growth from highly purified HEWL solutions, however, such inhomogeneities are much weaker and form only in response to unusually large changes in growth conditions. Equally important for connecting growth conditions to crystal perfection and diffraction resolution are recent advances in structural characterization through high-resolution Bragg reflection profiling and X-ray topography.</p></abstract><textClass><keywords scheme="keyword"><list><head>article-category</head><item><term>Section I. Keynote paper</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1996">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-D6FN0XNC-B/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>CRYS</jid><aid>96003582</aid><ce:pii>0022-0248(96)00358-2</ce:pii><ce:doi>10.1016/0022-0248(96)00358-2</ce:doi><ce:copyright type="unknown" year="1996"></ce:copyright><ce:doctopics><ce:doctopic><ce:text>Section I. Keynote paper</ce:text></ce:doctopic></ce:doctopics></item-info><head><ce:title>Nucleation and crystallization of globular proteins — what we know and what is missing</ce:title><ce:author-group><ce:author><ce:given-name>F.</ce:given-name><ce:surname>Rosenberger</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>P.G.</ce:given-name><ce:surname>Vekilov</ce:surname></ce:author><ce:author><ce:given-name>M.</ce:given-name><ce:surname>Muschol</ce:surname></ce:author><ce:author><ce:given-name>B.R.</ce:given-name><ce:surname>Thomas</ce:surname></ce:author><ce:affiliation><ce:textfn>Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Corresponding author.</ce:text></ce:correspondence></ce:author-group><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Recently, much progress has been made in understanding the nucleation and crystallization of globular proteins, including the formation of compositional and structural crystal defects. Insight into the interactions of (screened) protein macro-ions in solution, obtained from light scattering, small angle X-ray scattering and osmotic pressure studies, can guide the search for crystallization conditions. These studies show that the nucleation of globular proteins is governed by the same principles as that of small molecules. However, failure to account for direct and indirect (hydrodynamic) protein interactions in the solutions results in unrealistic aggregation scenarios. Microscopic studies of numerous proteins reveal that crystals grow by the attachment of growth units through the same layer-spreading mechanisms as inorganic crystals. Investigations of the growth kinetics of hen-egg-white lysozyme (HEWL) reveal non-steady behavior under steady external conditions. Long-term variations in growth rates are due to changes in step-originating dislocation groups. Fluctuations on a shorter timescale reflect the non-linear dynamics of layer growth that results from the interplay between interfacial kinetics and bulk transport. Systematic gel electrophoretic analyses suggest that most HEWL crystallization studies have been performed with material containing other proteins at percent levels. Yet, sub-percent levels of protein impurities impede growth step propagation and play a role in the formation of structural/compositional inhomogeneities. In crystal growth from highly purified HEWL solutions, however, such inhomogeneities are much weaker and form only in response to unusually large changes in growth conditions. 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Insight into the interactions of (screened) protein macro-ions in solution, obtained from light scattering, small angle X-ray scattering and osmotic pressure studies, can guide the search for crystallization conditions. These studies show that the nucleation of globular proteins is governed by the same principles as that of small molecules. However, failure to account for direct and indirect (hydrodynamic) protein interactions in the solutions results in unrealistic aggregation scenarios. Microscopic studies of numerous proteins reveal that crystals grow by the attachment of growth units through the same layer-spreading mechanisms as inorganic crystals. Investigations of the growth kinetics of hen-egg-white lysozyme (HEWL) reveal non-steady behavior under steady external conditions. Long-term variations in growth rates are due to changes in step-originating dislocation groups. Fluctuations on a shorter timescale reflect the non-linear dynamics of layer growth that results from the interplay between interfacial kinetics and bulk transport. Systematic gel electrophoretic analyses suggest that most HEWL crystallization studies have been performed with material containing other proteins at percent levels. Yet, sub-percent levels of protein impurities impede growth step propagation and play a role in the formation of structural/compositional inhomogeneities. In crystal growth from highly purified HEWL solutions, however, such inhomogeneities are much weaker and form only in response to unusually large changes in growth conditions. Equally important for connecting growth conditions to crystal perfection and diffraction resolution are recent advances in structural characterization through high-resolution Bragg reflection profiling and X-ray topography.</abstract><subject><genre>article-category</genre><topic>Section I. Keynote paper</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Crystal Growth</title></titleInfo><titleInfo type="abbreviated"><title>CRYS</title></titleInfo><name type="conference"><namePart>Crystallization of Biological Macromolecules, Hiroshima, Japan</namePart><namePart type="date">19951112</namePart><namePart type="date">19951117</namePart></name><name type="personal"><namePart>K. Miki</namePart><role><roleTerm type="text">editor</roleTerm></role></name><name type="personal"><namePart>M. Ataka</namePart><role><roleTerm type="text">editor</roleTerm></role></name><name type="personal"><namePart>K. Fukuyama</namePart><role><roleTerm type="text">editor</roleTerm></role></name><name type="personal"><namePart>Y. Higuchi</namePart><role><roleTerm type="text">editor</roleTerm></role></name><name type="personal"><namePart>T. 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