Separating nucleation and growth in protein crystallization using dynamic light scattering.
Identifieur interne : 000484 ( Main/Exploration ); précédent : 000483; suivant : 000485Separating nucleation and growth in protein crystallization using dynamic light scattering.
Auteurs : Emmanuel Saridakis [Royaume-Uni] ; Karsten Dierks ; Abel Moreno ; Matthias W M. Dieckmann ; Naomi E. ChayenSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2002.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Protéines, Protéines végétales, Trypsine, Édulcorants.
- méthodes : Cristallisation.
- Animaux, Diffusion de rayonnements, Lumière, Solutions, Taille de particule.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Plant Proteins, Proteins, Sweetening Agents, Trypsin.
- methods : Crystallization.
- Animals, Light, Particle Size, Scattering, Radiation, Solutions.
Abstract
A means of controlling crystallization is to separate the phases of nucleation and growth. Methods to achieve this, other than seeding, involve lowering the supersaturation by changing the temperature or diluting drops after incubating them for a given time at nucleation conditions. However, by the time nuclei or crystals are visible under the microscope too many nuclei will have formed. Dynamic Light Scattering was applied practically, to determine the most likely time for nucleation-growth decoupling to be performed successfully. The time at which DLS showed a significant change in the size-distribution of species in solution, corresponded to that optimal time.
DOI: 10.1107/s0907444902014348
PubMed: 12351869
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Dieckmann</name></author><author><name sortKey="Chayen, Naomi E" sort="Chayen, Naomi E" uniqKey="Chayen N" first="Naomi E" last="Chayen">Naomi E. Chayen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:12351869</idno><idno type="pmid">12351869</idno><idno type="doi">10.1107/s0907444902014348</idno><idno type="wicri:Area/Main/Corpus">000491</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000491</idno><idno type="wicri:Area/Main/Curation">000491</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000491</idno><idno type="wicri:Area/Main/Exploration">000491</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Separating nucleation and growth in protein crystallization using dynamic light scattering.</title><author><name sortKey="Saridakis, Emmanuel" sort="Saridakis, Emmanuel" uniqKey="Saridakis E" first="Emmanuel" last="Saridakis">Emmanuel Saridakis</name><affiliation wicri:level="1"><nlm:affiliation>Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ</wicri:regionArea><wicri:noRegion>London SW7 2AZ</wicri:noRegion></affiliation></author><author><name sortKey="Dierks, Karsten" sort="Dierks, Karsten" uniqKey="Dierks K" first="Karsten" last="Dierks">Karsten Dierks</name></author><author><name sortKey="Moreno, Abel" sort="Moreno, Abel" uniqKey="Moreno A" first="Abel" last="Moreno">Abel Moreno</name></author><author><name sortKey="Dieckmann, Matthias W M" sort="Dieckmann, Matthias W M" uniqKey="Dieckmann M" first="Matthias W M" last="Dieckmann">Matthias W M. Dieckmann</name></author><author><name sortKey="Chayen, Naomi E" sort="Chayen, Naomi E" uniqKey="Chayen N" first="Naomi E" last="Chayen">Naomi E. Chayen</name></author></analytic><series><title level="j">Acta crystallographica. Section D, Biological crystallography</title><idno type="ISSN">0907-4449</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Crystallization (methods)</term><term>Light (MeSH)</term><term>Particle Size (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Proteins (chemistry)</term><term>Scattering, Radiation (MeSH)</term><term>Solutions (MeSH)</term><term>Sweetening Agents (chemistry)</term><term>Trypsin (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cristallisation (méthodes)</term><term>Diffusion de rayonnements (MeSH)</term><term>Lumière (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines végétales (composition chimique)</term><term>Solutions (MeSH)</term><term>Taille de particule (MeSH)</term><term>Trypsine (composition chimique)</term><term>Édulcorants (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term><term>Proteins</term><term>Sweetening Agents</term><term>Trypsin</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines</term><term>Protéines végétales</term><term>Trypsine</term><term>Édulcorants</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallization</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Cristallisation</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Light</term><term>Particle Size</term><term>Scattering, Radiation</term><term>Solutions</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Diffusion de rayonnements</term><term>Lumière</term><term>Solutions</term><term>Taille de particule</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A means of controlling crystallization is to separate the phases of nucleation and growth. Methods to achieve this, other than seeding, involve lowering the supersaturation by changing the temperature or diluting drops after incubating them for a given time at nucleation conditions. However, by the time nuclei or crystals are visible under the microscope too many nuclei will have formed. Dynamic Light Scattering was applied practically, to determine the most likely time for nucleation-growth decoupling to be performed successfully. The time at which DLS showed a significant change in the size-distribution of species in solution, corresponded to that optimal time.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12351869</PMID><DateCompleted><Year>2003</Year><Month>03</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0907-4449</ISSN><JournalIssue CitedMedium="Print"><Volume>58</Volume><Issue>Pt 10 Pt 1</Issue><PubDate><Year>2002</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>Separating nucleation and growth in protein crystallization using dynamic light scattering.</ArticleTitle><Pagination><MedlinePgn>1597-600</MedlinePgn></Pagination><Abstract><AbstractText>A means of controlling crystallization is to separate the phases of nucleation and growth. Methods to achieve this, other than seeding, involve lowering the supersaturation by changing the temperature or diluting drops after incubating them for a given time at nucleation conditions. However, by the time nuclei or crystals are visible under the microscope too many nuclei will have formed. Dynamic Light Scattering was applied practically, to determine the most likely time for nucleation-growth decoupling to be performed successfully. The time at which DLS showed a significant change in the size-distribution of species in solution, corresponded to that optimal time.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Saridakis</LastName><ForeName>Emmanuel</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Biological Structure and Function Section, Division of Biomedical Sciences, Faculty of Medicine, Imperial College, London SW7 2AZ, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dierks</LastName><ForeName>Karsten</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Moreno</LastName><ForeName>Abel</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Dieckmann</LastName><ForeName>Matthias W M</ForeName><Initials>MW</Initials></Author><Author ValidYN="Y"><LastName>Chayen</LastName><ForeName>Naomi E</ForeName><Initials>NE</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2002</Year><Month>09</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Biol Crystallogr</MedlineTA><NlmUniqueID>9305878</NlmUniqueID><ISSNLinking>0907-4449</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012996">Solutions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013549">Sweetening Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008027" MajorTopicYN="N">Light</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010316" MajorTopicYN="N">Particle Size</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012542" MajorTopicYN="N">Scattering, Radiation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012996" MajorTopicYN="N">Solutions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013549" MajorTopicYN="N">Sweetening Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2002</Year><Month>03</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2002</Year><Month>08</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>9</Month><Day>28</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>3</Month><Day>18</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>9</Month><Day>28</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12351869</ArticleId><ArticleId IdType="pii">S0907444902014348</ArticleId><ArticleId IdType="doi">10.1107/s0907444902014348</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><noCountry><name sortKey="Chayen, Naomi E" sort="Chayen, Naomi E" uniqKey="Chayen N" first="Naomi E" last="Chayen">Naomi E. Chayen</name><name sortKey="Dieckmann, Matthias W M" sort="Dieckmann, Matthias W M" uniqKey="Dieckmann M" first="Matthias W M" last="Dieckmann">Matthias W M. Dieckmann</name><name sortKey="Dierks, Karsten" sort="Dierks, Karsten" uniqKey="Dierks K" first="Karsten" last="Dierks">Karsten Dierks</name><name sortKey="Moreno, Abel" sort="Moreno, Abel" uniqKey="Moreno A" first="Abel" last="Moreno">Abel Moreno</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Saridakis, Emmanuel" sort="Saridakis, Emmanuel" uniqKey="Saridakis E" first="Emmanuel" last="Saridakis">Emmanuel Saridakis</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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