Towards protein-crystal centering using second-harmonic generation (SHG) microscopy.
Identifieur interne : 000181 ( Main/Exploration ); précédent : 000180; suivant : 000182Towards protein-crystal centering using second-harmonic generation (SHG) microscopy.
Auteurs : David J. Kissick [États-Unis] ; Christopher M. Dettmar ; Michael Becker ; Anne M. Mulichak ; Vadim Cherezov ; Stephan L. Ginell ; Kevin P. Battaile ; Lisa J. Keefe ; Robert F. Fischetti ; Garth J. SimpsonSource :
- Acta crystallographica. Section D, Biological crystallography [ 1399-0047 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (instrumentation), Cristallographie aux rayons X (méthodes), Diffraction des rayons X (MeSH), Equus caballus (MeSH), Microscopie (méthodes), Myoglobine (composition chimique), Protéines (composition chimique), Récepteurs bêta-2 adrénergiques (composition chimique), Synchrotrons (MeSH), Traitement d'image par ordinateur (MeSH).
- MESH :
- composition chimique : Myoglobine, Protéines, Récepteurs bêta-2 adrénergiques.
- méthodes : Cristallographie aux rayons X, Microscopie.
- instrumentation : Animaux, Conformation des protéines, Cristallographie aux rayons X, Diffraction des rayons X, Equus caballus, Synchrotrons, Traitement d'image par ordinateur.
English descriptors
- KwdEn :
- Animals (MeSH), Crystallography, X-Ray (instrumentation), Crystallography, X-Ray (methods), Horses (MeSH), Image Processing, Computer-Assisted (MeSH), Microscopy (methods), Myoglobin (chemistry), Protein Conformation (MeSH), Proteins (chemistry), Receptors, Adrenergic, beta-2 (chemistry), Synchrotrons (MeSH), X-Ray Diffraction (MeSH).
- MESH :
- chemical , chemistry : Myoglobin, Proteins, Receptors, Adrenergic, beta-2.
- instrumentation : Crystallography, X-Ray.
- methods : Crystallography, X-Ray, Microscopy.
- Animals, Horses, Image Processing, Computer-Assisted, Protein Conformation, Synchrotrons, X-Ray Diffraction.
Abstract
The potential of second-harmonic generation (SHG) microscopy for automated crystal centering to guide synchrotron X-ray diffraction of protein crystals was explored. These studies included (i) comparison of microcrystal positions in cryoloops as determined by SHG imaging and by X-ray diffraction rastering and (ii) X-ray structure determinations of selected proteins to investigate the potential for laser-induced damage from SHG imaging. In studies using β2 adrenergic receptor membrane-protein crystals prepared in lipidic mesophase, the crystal locations identified by SHG images obtained in transmission mode were found to correlate well with the crystal locations identified by raster scanning using an X-ray minibeam. SHG imaging was found to provide about 2 µm spatial resolution and shorter image-acquisition times. The general insensitivity of SHG images to optical scatter enabled the reliable identification of microcrystals within opaque cryocooled lipidic mesophases that were not identified by conventional bright-field imaging. The potential impact of extended exposure of protein crystals to five times a typical imaging dose from an ultrafast laser source was also assessed. Measurements of myoglobin and thaumatin crystals resulted in no statistically significant differences between structures obtained from diffraction data acquired from exposed and unexposed regions of single crystals. Practical constraints for integrating SHG imaging into an active beamline for routine automated crystal centering are discussed.
DOI: 10.1107/S0907444913002746
PubMed: 23633594
PubMed Central: PMC3640472
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Mulichak</name></author><author><name sortKey="Cherezov, Vadim" sort="Cherezov, Vadim" uniqKey="Cherezov V" first="Vadim" last="Cherezov">Vadim Cherezov</name></author><author><name sortKey="Ginell, Stephan L" sort="Ginell, Stephan L" uniqKey="Ginell S" first="Stephan L" last="Ginell">Stephan L. Ginell</name></author><author><name sortKey="Battaile, Kevin P" sort="Battaile, Kevin P" uniqKey="Battaile K" first="Kevin P" last="Battaile">Kevin P. Battaile</name></author><author><name sortKey="Keefe, Lisa J" sort="Keefe, Lisa J" uniqKey="Keefe L" first="Lisa J" last="Keefe">Lisa J. Keefe</name></author><author><name sortKey="Fischetti, Robert F" sort="Fischetti, Robert F" uniqKey="Fischetti R" first="Robert F" last="Fischetti">Robert F. Fischetti</name></author><author><name sortKey="Simpson, Garth J" sort="Simpson, Garth J" uniqKey="Simpson G" first="Garth J" last="Simpson">Garth J. Simpson</name></author></analytic><series><title level="j">Acta crystallographica. Section D, Biological crystallography</title><idno type="eISSN">1399-0047</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Crystallography, X-Ray (instrumentation)</term><term>Crystallography, X-Ray (methods)</term><term>Horses (MeSH)</term><term>Image Processing, Computer-Assisted (MeSH)</term><term>Microscopy (methods)</term><term>Myoglobin (chemistry)</term><term>Protein Conformation (MeSH)</term><term>Proteins (chemistry)</term><term>Receptors, Adrenergic, beta-2 (chemistry)</term><term>Synchrotrons (MeSH)</term><term>X-Ray Diffraction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (instrumentation)</term><term>Cristallographie aux rayons X (méthodes)</term><term>Diffraction des rayons X (MeSH)</term><term>Equus caballus (MeSH)</term><term>Microscopie (méthodes)</term><term>Myoglobine (composition chimique)</term><term>Protéines (composition chimique)</term><term>Récepteurs bêta-2 adrénergiques (composition chimique)</term><term>Synchrotrons (MeSH)</term><term>Traitement d'image par ordinateur (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Myoglobin</term><term>Proteins</term><term>Receptors, Adrenergic, beta-2</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Myoglobine</term><term>Protéines</term><term>Récepteurs bêta-2 adrénergiques</term></keywords><keywords scheme="MESH" qualifier="instrumentation" xml:lang="en"><term>Crystallography, X-Ray</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallography, X-Ray</term><term>Microscopy</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Cristallographie aux rayons X</term><term>Microscopie</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Horses</term><term>Image Processing, Computer-Assisted</term><term>Protein Conformation</term><term>Synchrotrons</term><term>X-Ray Diffraction</term></keywords><keywords scheme="MESH" qualifier="instrumentation" xml:lang="fr"><term>Animaux</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Diffraction des rayons X</term><term>Equus caballus</term><term>Synchrotrons</term><term>Traitement d'image par ordinateur</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The potential of second-harmonic generation (SHG) microscopy for automated crystal centering to guide synchrotron X-ray diffraction of protein crystals was explored. These studies included (i) comparison of microcrystal positions in cryoloops as determined by SHG imaging and by X-ray diffraction rastering and (ii) X-ray structure determinations of selected proteins to investigate the potential for laser-induced damage from SHG imaging. In studies using β2 adrenergic receptor membrane-protein crystals prepared in lipidic mesophase, the crystal locations identified by SHG images obtained in transmission mode were found to correlate well with the crystal locations identified by raster scanning using an X-ray minibeam. SHG imaging was found to provide about 2 µm spatial resolution and shorter image-acquisition times. The general insensitivity of SHG images to optical scatter enabled the reliable identification of microcrystals within opaque cryocooled lipidic mesophases that were not identified by conventional bright-field imaging. The potential impact of extended exposure of protein crystals to five times a typical imaging dose from an ultrafast laser source was also assessed. Measurements of myoglobin and thaumatin crystals resulted in no statistically significant differences between structures obtained from diffraction data acquired from exposed and unexposed regions of single crystals. Practical constraints for integrating SHG imaging into an active beamline for routine automated crystal centering are discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23633594</PMID><DateCompleted><Year>2014</Year><Month>01</Month><Day>28</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>11</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1399-0047</ISSN><JournalIssue CitedMedium="Internet"><Volume>69</Volume><Issue>Pt 5</Issue><PubDate><Year>2013</Year><Month>May</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>Towards protein-crystal centering using second-harmonic generation (SHG) microscopy.</ArticleTitle><Pagination><MedlinePgn>843-51</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S0907444913002746</ELocationID><Abstract><AbstractText>The potential of second-harmonic generation (SHG) microscopy for automated crystal centering to guide synchrotron X-ray diffraction of protein crystals was explored. These studies included (i) comparison of microcrystal positions in cryoloops as determined by SHG imaging and by X-ray diffraction rastering and (ii) X-ray structure determinations of selected proteins to investigate the potential for laser-induced damage from SHG imaging. In studies using β2 adrenergic receptor membrane-protein crystals prepared in lipidic mesophase, the crystal locations identified by SHG images obtained in transmission mode were found to correlate well with the crystal locations identified by raster scanning using an X-ray minibeam. SHG imaging was found to provide about 2 µm spatial resolution and shorter image-acquisition times. The general insensitivity of SHG images to optical scatter enabled the reliable identification of microcrystals within opaque cryocooled lipidic mesophases that were not identified by conventional bright-field imaging. The potential impact of extended exposure of protein crystals to five times a typical imaging dose from an ultrafast laser source was also assessed. Measurements of myoglobin and thaumatin crystals resulted in no statistically significant differences between structures obtained from diffraction data acquired from exposed and unexposed regions of single crystals. Practical constraints for integrating SHG imaging into an active beamline for routine automated crystal centering are discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kissick</LastName><ForeName>David J</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dettmar</LastName><ForeName>Christopher M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Becker</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Mulichak</LastName><ForeName>Anne M</ForeName><Initials>AM</Initials></Author><Author ValidYN="Y"><LastName>Cherezov</LastName><ForeName>Vadim</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Ginell</LastName><ForeName>Stephan L</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Battaile</LastName><ForeName>Kevin P</ForeName><Initials>KP</Initials></Author><Author ValidYN="Y"><LastName>Keefe</LastName><ForeName>Lisa J</ForeName><Initials>LJ</Initials></Author><Author ValidYN="Y"><LastName>Fischetti</LastName><ForeName>Robert F</ForeName><Initials>RF</Initials></Author><Author ValidYN="Y"><LastName>Simpson</LastName><ForeName>Garth J</ForeName><Initials>GJ</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>4DC5</AccessionNumber><AccessionNumber>4DC6</AccessionNumber><AccessionNumber>4DC7</AccessionNumber><AccessionNumber>4DC8</AccessionNumber></AccessionNumberList></DataBank></DataBankList><GrantList CompleteYN="Y"><Grant><GrantID>P50 GM073197</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM103401</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01GM103401</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>Y1-GM-1104</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>04</Month><Day>19</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="D009211">Myoglobin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018343">Receptors, Adrenergic, beta-2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName><QualifierName UI="Q000295" MajorTopicYN="N">instrumentation</QualifierName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006736" MajorTopicYN="N">Horses</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007091" MajorTopicYN="N">Image Processing, Computer-Assisted</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008853" MajorTopicYN="N">Microscopy</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009211" MajorTopicYN="N">Myoglobin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018343" MajorTopicYN="N">Receptors, Adrenergic, beta-2</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017356" MajorTopicYN="N">Synchrotrons</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014961" MajorTopicYN="N">X-Ray Diffraction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">crystal centering</Keyword><Keyword MajorTopicYN="N">imaging</Keyword><Keyword MajorTopicYN="N">second-harmonic generation microscopy</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>06</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>01</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>5</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>5</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Battaile</name><name sortKey="Becker, Michael" sort="Becker, Michael" uniqKey="Becker M" first="Michael" last="Becker">Michael Becker</name><name sortKey="Cherezov, Vadim" sort="Cherezov, Vadim" uniqKey="Cherezov V" first="Vadim" last="Cherezov">Vadim Cherezov</name><name sortKey="Dettmar, Christopher M" sort="Dettmar, Christopher M" uniqKey="Dettmar C" first="Christopher M" last="Dettmar">Christopher M. Dettmar</name><name sortKey="Fischetti, Robert F" sort="Fischetti, Robert F" uniqKey="Fischetti R" first="Robert F" last="Fischetti">Robert F. Fischetti</name><name sortKey="Ginell, Stephan L" sort="Ginell, Stephan L" uniqKey="Ginell S" first="Stephan L" last="Ginell">Stephan L. Ginell</name><name sortKey="Keefe, Lisa J" sort="Keefe, Lisa J" uniqKey="Keefe L" first="Lisa J" last="Keefe">Lisa J. Keefe</name><name sortKey="Mulichak, Anne M" sort="Mulichak, Anne M" uniqKey="Mulichak A" first="Anne M" last="Mulichak">Anne M. Mulichak</name><name sortKey="Simpson, Garth J" sort="Simpson, Garth J" uniqKey="Simpson G" first="Garth J" last="Simpson">Garth J. Simpson</name></noCountry><country name="États-Unis"><region name="Indiana"><name sortKey="Kissick, David J" sort="Kissick, David J" uniqKey="Kissick D" first="David J" last="Kissick">David J. Kissick</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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