Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b 6 f complexes
Identifieur interne : 002065 ( Istex/Corpus ); précédent : 002064; suivant : 002066Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b 6 f complexes
Auteurs : C. Tribet ; D. Mills ; M. Haider ; J. L. PopotSource :
- Biochimie [ 0300-9084 ] ; 1998.
English descriptors
- Teeft :
- Aggregation, Aggregation state, Amac, Ammonium acetate, Ammonium buffer, Amphipol, Amphipol binding, Amphipol stock solution, Amphipols, Aqueous solutions, Biochemical composition, Centrifugation, Comparative study, Complexation, Conventional detergents, Cytochrome, Cytochrome complexes, Detergent solution, Detergent solutions, Electron microscopy, Excess amphipols, Excess lipids, Final complexes, Free amphipols, Heavy form, Hydroxylapatite column, Integral membrane proteins, Interesting perspectives, Light form, Lipid, Lipid binding, Liquid helium temperature, Mass analysis, Mass determination, Mass distribution, Membrane proteins, Molecular mass, Native form, Other hand, Polymer, Present address, Present article, Present study, Protease inhibitors, Purification protocols, Rate zonal centrifugation analysis, Rieske, Rieske protein, Rieske subunit, Scanning transmission electron microscopy, Stock solution, Subunit, Subunit petl, Sucrose, Sucrose gradient, Sucrose gradients, Tobacco mosaic virus, Unpublished observations.
Abstract
Abstract: The composition and mass of complexes between Chlamydomonas reinhardtii cytochrome b6f and low molecular mass amphipathic polymers (‘amphipols’) have been studied using biochemical analysis and scanning transmission electron microscopy at liquid helium temperature (cryo-STEM). Cytochrome b6f was trapped by amphipols either under its native 14-meric state or as a delipidated, lighter form. A good consistency was observed between the masses of either form calculated from their biochemical composition and those determined by cryo-STEM. These data show that association with amphipols preserved the original aggregation state of the protein in detergent solution. Complexation with amphipols appears to facilitate preparation of the samples and mass determination by cryo-STEM as compared to conventional solubilization with detergents.
Url:
DOI: 10.1016/S0300-9084(00)80014-0
Links to Exploration step
ISTEX:6C866A5375E3317494F2D755131C3F4F6729159BLe document en format XML
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Mills</name><affiliation><mods:affiliation>European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>∗∗ Present address: Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Straße 7, 60528 Frankfurt-am-Main, Germany.</mods:affiliation></affiliation></author><author><name sortKey="Haider, M" sort="Haider, M" uniqKey="Haider M" first="M." last="Haider">M. Haider</name><affiliation><mods:affiliation>European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>∗∗∗ Present address: CEOS GmbH, hn Neuenheimer Feld 519, 69120 Heidelberg, Germany.</mods:affiliation></affiliation></author><author><name sortKey="Popot, J L" sort="Popot, J L" uniqKey="Popot J" first="J. L." last="Popot">J. L. 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Tribet</name><affiliation><mods:affiliation>CNRS-UMR 7615 and Université Paris-6, École Supérieure de Physique et de Chimie Industrielles, 10, rue Vanquelin, F-75231 Paris cedex 05, France</mods:affiliation></affiliation></author><author><name sortKey="Mills, D" sort="Mills, D" uniqKey="Mills D" first="D." last="Mills">D. Mills</name><affiliation><mods:affiliation>European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>∗∗ Present address: Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Straße 7, 60528 Frankfurt-am-Main, Germany.</mods:affiliation></affiliation></author><author><name sortKey="Haider, M" sort="Haider, M" uniqKey="Haider M" first="M." last="Haider">M. Haider</name><affiliation><mods:affiliation>European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>∗∗∗ Present address: CEOS GmbH, hn Neuenheimer Feld 519, 69120 Heidelberg, Germany.</mods:affiliation></affiliation></author><author><name sortKey="Popot, J L" sort="Popot, J L" uniqKey="Popot J" first="J. L." last="Popot">J. L. Popot</name><affiliation><mods:affiliation>Correspondence and reprints.</mods:affiliation></affiliation><affiliation><mods:affiliation>CNRS-UPR 9052 and Université Paris-7, Institut de Biologie Physico-Chimique, 13, rue P-et-M-Curie, F-75005 Paris cedex 05, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochimie</title><title level="j" type="abbrev">BIOCHI</title><idno type="ISSN">0300-9084</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">80</biblScope><biblScope unit="issue">5–6</biblScope><biblScope unit="page" from="475">475</biblScope><biblScope unit="page" to="482">482</biblScope></imprint><idno type="ISSN">0300-9084</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0300-9084</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Aggregation</term><term>Aggregation state</term><term>Amac</term><term>Ammonium acetate</term><term>Ammonium buffer</term><term>Amphipol</term><term>Amphipol binding</term><term>Amphipol stock solution</term><term>Amphipols</term><term>Aqueous solutions</term><term>Biochemical composition</term><term>Centrifugation</term><term>Comparative study</term><term>Complexation</term><term>Conventional detergents</term><term>Cytochrome</term><term>Cytochrome complexes</term><term>Detergent solution</term><term>Detergent solutions</term><term>Electron microscopy</term><term>Excess amphipols</term><term>Excess lipids</term><term>Final complexes</term><term>Free amphipols</term><term>Heavy form</term><term>Hydroxylapatite column</term><term>Integral membrane proteins</term><term>Interesting perspectives</term><term>Light form</term><term>Lipid</term><term>Lipid binding</term><term>Liquid helium temperature</term><term>Mass analysis</term><term>Mass determination</term><term>Mass distribution</term><term>Membrane proteins</term><term>Molecular mass</term><term>Native form</term><term>Other hand</term><term>Polymer</term><term>Present address</term><term>Present article</term><term>Present study</term><term>Protease inhibitors</term><term>Purification protocols</term><term>Rate zonal centrifugation analysis</term><term>Rieske</term><term>Rieske protein</term><term>Rieske subunit</term><term>Scanning transmission electron microscopy</term><term>Stock solution</term><term>Subunit</term><term>Subunit petl</term><term>Sucrose</term><term>Sucrose gradient</term><term>Sucrose gradients</term><term>Tobacco mosaic virus</term><term>Unpublished observations</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The composition and mass of complexes between Chlamydomonas reinhardtii cytochrome b6f and low molecular mass amphipathic polymers (‘amphipols’) have been studied using biochemical analysis and scanning transmission electron microscopy at liquid helium temperature (cryo-STEM). Cytochrome b6f was trapped by amphipols either under its native 14-meric state or as a delipidated, lighter form. A good consistency was observed between the masses of either form calculated from their biochemical composition and those determined by cryo-STEM. These data show that association with amphipols preserved the original aggregation state of the protein in detergent solution. Complexation with amphipols appears to facilitate preparation of the samples and mass determination by cryo-STEM as compared to conventional solubilization with detergents.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>lipid</json:string><json:string>amphipols</json:string><json:string>cytochrome</json:string><json:string>sucrose</json:string><json:string>amphipol</json:string><json:string>heavy form</json:string><json:string>subunit</json:string><json:string>light form</json:string><json:string>membrane proteins</json:string><json:string>sucrose gradient</json:string><json:string>sucrose gradients</json:string><json:string>rieske</json:string><json:string>molecular mass</json:string><json:string>amac</json:string><json:string>complexation</json:string><json:string>aggregation</json:string><json:string>detergent solution</json:string><json:string>polymer</json:string><json:string>excess lipids</json:string><json:string>liquid helium temperature</json:string><json:string>rieske protein</json:string><json:string>stock solution</json:string><json:string>unpublished observations</json:string><json:string>free amphipols</json:string><json:string>scanning transmission electron microscopy</json:string><json:string>rate zonal centrifugation analysis</json:string><json:string>centrifugation</json:string><json:string>biochemical composition</json:string><json:string>present article</json:string><json:string>mass determination</json:string><json:string>conventional detergents</json:string><json:string>aggregation state</json:string><json:string>native form</json:string><json:string>other hand</json:string><json:string>detergent solutions</json:string><json:string>ammonium acetate</json:string><json:string>cytochrome complexes</json:string><json:string>present address</json:string><json:string>comparative study</json:string><json:string>hydroxylapatite column</json:string><json:string>ammonium buffer</json:string><json:string>protease inhibitors</json:string><json:string>subunit petl</json:string><json:string>final complexes</json:string><json:string>lipid binding</json:string><json:string>amphipol stock solution</json:string><json:string>integral membrane proteins</json:string><json:string>electron microscopy</json:string><json:string>rieske subunit</json:string><json:string>excess amphipols</json:string><json:string>tobacco mosaic virus</json:string><json:string>mass distribution</json:string><json:string>mass analysis</json:string><json:string>present study</json:string><json:string>purification protocols</json:string><json:string>interesting perspectives</json:string><json:string>aqueous solutions</json:string><json:string>amphipol binding</json:string></teeft></keywords><author><json:item><name>C. Tribet</name><affiliations><json:string>CNRS-UMR 7615 and Université Paris-6, École Supérieure de Physique et de Chimie Industrielles, 10, rue Vanquelin, F-75231 Paris cedex 05, France</json:string></affiliations></json:item><json:item><name>D. Mills</name><affiliations><json:string>European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany</json:string><json:string>∗∗ Present address: Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Straße 7, 60528 Frankfurt-am-Main, Germany.</json:string></affiliations></json:item><json:item><name>M. Haider</name><affiliations><json:string>European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany</json:string><json:string>∗∗∗ Present address: CEOS GmbH, hn Neuenheimer Feld 519, 69120 Heidelberg, Germany.</json:string></affiliations></json:item><json:item><name>J.L. Popot</name><affiliations><json:string>Correspondence and reprints.</json:string><json:string>CNRS-UPR 9052 and Université Paris-7, Institut de Biologie Physico-Chimique, 13, rue P-et-M-Curie, F-75005 Paris cedex 05, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>membrane proteins</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>detergents</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>amphipols</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>electron microscopy</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cytochrome b6f</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>AmAc, ammonium acetate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>AP, ammonium phosphate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cryo-STEM, scanning transmission electron microscopy at liquid helium temperature</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cmc, critical micellar concentration</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DPPC, dipalmitoylphosphatidylcholine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>EM, electron microscopy</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HG, 6-O-(N-heptylcarbamoyl)-methyl-α-D-glycopyranoside (Hecameg)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>LM, dodecyl-β-D-maltoside (laurylmaltoside)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Mr, molecular mass</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PC, phosphatidylcholine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>SDS-PAGE, polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>STEM, scanning transmission electron microscopy</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>TMV, tobacco mosaic virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Tricine, N-tris (hydroxymethyl)methylglycine</value></json:item></subject><arkIstex>ark:/67375/6H6-G4CKWCNR-H</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The composition and mass of complexes between Chlamydomonas reinhardtii cytochrome b6f and low molecular mass amphipathic polymers (‘amphipols’) have been studied using biochemical analysis and scanning transmission electron microscopy at liquid helium temperature (cryo-STEM). Cytochrome b6f was trapped by amphipols either under its native 14-meric state or as a delipidated, lighter form. A good consistency was observed between the masses of either form calculated from their biochemical composition and those determined by cryo-STEM. These data show that association with amphipols preserved the original aggregation state of the protein in detergent solution. Complexation with amphipols appears to facilitate preparation of the samples and mass determination by cryo-STEM as compared to conventional solubilization with detergents.</abstract><qualityIndicators><score>8.368</score><pdfWordCount>5228</pdfWordCount><pdfCharCount>32616</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>648 x 828 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>114</abstractWordCount><abstractCharCount>848</abstractCharCount><keywordCount>19</keywordCount></qualityIndicators><title>Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b 6 f complexes</title><pmid><json:string>9782387</json:string></pmid><pii><json:string>S0300-9084(00)80014-0</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc Natl Acad Sci USA</title><language><json:string>unknown</json:string></language><volume>93</volume><pages><first>15047</first><last>15050</last></pages></serie><host><title>Biochimie</title><language><json:string>unknown</json:string></language><publicationDate>1998</publicationDate><issn><json:string>0300-9084</json:string></issn><pii><json:string>S0300-9084(00)X0056-9</json:string></pii><volume>80</volume><issue>5–6</issue><pages><first>475</first><last>482</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>5000</json:string><json:string>1998</json:string></date><geogName></geogName><orgName><json:string>CNRS</json:string></orgName><orgName_funder><json:string>CNRS</json:string></orgName_funder><orgName_provider></orgName_provider><persName></persName><placeName><json:string>Germany</json:string><json:string>Heidelberg</json:string><json:string>Frankfurt</json:string><json:string>France</json:string><json:string>COmo</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[4]</json:string><json:string>[3, 4]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-G4CKWCNR-H</json:string></ark><categories><wos><json:string>1 - 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Cytochrome b6f was trapped by amphipols either under its native 14-meric state or as a delipidated, lighter form. A good consistency was observed between the masses of either form calculated from their biochemical composition and those determined by cryo-STEM. These data show that association with amphipols preserved the original aggregation state of the protein in detergent solution. Complexation with amphipols appears to facilitate preparation of the samples and mass determination by cryo-STEM as compared to conventional solubilization with detergents.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>membrane proteins</term></item><item><term>detergents</term></item><item><term>amphipols</term></item><item><term>electron microscopy</term></item><item><term>cytochrome b6f</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>AmAc, ammonium acetate</term></item><item><term>AP, ammonium phosphate</term></item><item><term>cryo-STEM, scanning transmission electron microscopy at liquid helium temperature</term></item><item><term>cmc, critical micellar concentration</term></item><item><term>DPPC, dipalmitoylphosphatidylcholine</term></item><item><term>EM, electron microscopy</term></item><item><term>HG, 6-O-(N-heptylcarbamoyl)-methyl-α-D-glycopyranoside (Hecameg)</term></item><item><term>LM, dodecyl-β-D-maltoside (laurylmaltoside)</term></item><item><term>Mr, molecular mass</term></item><item><term>PC, phosphatidylcholine</term></item><item><term>SDS-PAGE, polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate</term></item><item><term>STEM, scanning transmission electron microscopy</term></item><item><term>TMV, tobacco mosaic virus</term></item><item><term>Tricine, N-tris (hydroxymethyl)methylglycine</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998">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-G4CKWCNR-H/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>BIOCHI</jid><aid>00800140</aid><ce:pii>S0300-9084(00)80014-0</ce:pii><ce:doi>10.1016/S0300-9084(00)80014-0</ce:doi><ce:copyright type="unknown" year="1998"></ce:copyright></item-info><head><ce:title>Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome <ce:italic>b</ce:italic><ce:inf>6</ce:inf><ce:italic>f</ce:italic> complexes</ce:title><ce:author-group><ce:author><ce:given-name>C.</ce:given-name><ce:surname>Tribet</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>D.</ce:given-name><ce:surname>Mills</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>∗∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>M.</ce:given-name><ce:surname>Haider</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref><ce:cross-ref refid="FN2"><ce:sup>∗∗∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>J.L.</ce:given-name><ce:surname>Popot</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF3"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>CNRS-UMR 7615 and Université Paris-6, École Supérieure de Physique et de Chimie Industrielles, 10, rue Vanquelin, F-75231 Paris cedex 05, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>CNRS-UPR 9052 and Université Paris-7, Institut de Biologie Physico-Chimique, 13, rue P-et-M-Curie, F-75005 Paris cedex 05, France</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Correspondence and reprints.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>∗∗</ce:label><ce:note-para>Present address: Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Straße 7, 60528 Frankfurt-am-Main, Germany.</ce:note-para></ce:footnote><ce:footnote id="FN2"><ce:label>∗∗∗</ce:label><ce:note-para>Present address: CEOS GmbH, hn Neuenheimer Feld 519, 69120 Heidelberg, Germany.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="23" month="12" year="1997"></ce:date-received><ce:date-accepted day="23" month="4" year="1998"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The composition and mass of complexes between <ce:italic>Chlamydomonas reinhardtii</ce:italic> cytochrome <ce:italic>b</ce:italic><ce:inf>6</ce:inf><ce:italic>f</ce:italic> and low molecular mass amphipathic polymers (‘amphipols’) have been studied using biochemical analysis and scanning transmission electron microscopy at liquid helium temperature (cryo-STEM). Cytochrome <ce:italic>b</ce:italic><ce:inf>6</ce:inf><ce:italic>f</ce:italic> was trapped by amphipols either under its native 14-meric state or as a delipidated, lighter form. A good consistency was observed between the masses of either form calculated from their biochemical composition and those determined by cryo-STEM. These data show that association with amphipols preserved the original aggregation state of the protein in detergent solution. Complexation with amphipols appears to facilitate preparation of the samples and mass determination by cryo-STEM as compared to conventional solubilization with detergents.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>membrane proteins</ce:text></ce:keyword><ce:keyword><ce:text>detergents</ce:text></ce:keyword><ce:keyword><ce:text>amphipols</ce:text></ce:keyword><ce:keyword><ce:text>electron microscopy</ce:text></ce:keyword><ce:keyword><ce:text>cytochrome <ce:italic>b</ce:italic><ce:inf>6</ce:inf><ce:italic>f</ce:italic></ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>AmAc, ammonium acetate</ce:text></ce:keyword><ce:keyword><ce:text>AP, ammonium phosphate</ce:text></ce:keyword><ce:keyword><ce:text>cryo-STEM, scanning transmission electron microscopy at liquid helium temperature</ce:text></ce:keyword><ce:keyword><ce:text>cmc, critical micellar concentration</ce:text></ce:keyword><ce:keyword><ce:text>DPPC, dipalmitoylphosphatidylcholine</ce:text></ce:keyword><ce:keyword><ce:text>EM, electron microscopy</ce:text></ce:keyword><ce:keyword><ce:text>HG, 6-<ce:italic>O</ce:italic>-(<ce:italic>N</ce:italic>-heptylcarbamoyl)-methyl-α-D-glycopyranoside (Hecameg)</ce:text></ce:keyword><ce:keyword><ce:text>LM, dodecyl-β-D-maltoside (laurylmaltoside)</ce:text></ce:keyword><ce:keyword><ce:text><ce:italic>M</ce:italic><ce:inf>r</ce:inf>, molecular mass</ce:text></ce:keyword><ce:keyword><ce:text>PC, phosphatidylcholine</ce:text></ce:keyword><ce:keyword><ce:text>SDS-PAGE, polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate</ce:text></ce:keyword><ce:keyword><ce:text>STEM, scanning transmission electron microscopy</ce:text></ce:keyword><ce:keyword><ce:text>TMV, tobacco mosaic virus</ce:text></ce:keyword><ce:keyword><ce:text>Tricine, <ce:italic>N</ce:italic>-tris (hydroxymethyl)methylglycine</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b 6 f complexes</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome</title></titleInfo><name type="personal"><namePart type="given">C.</namePart><namePart type="family">Tribet</namePart><affiliation>CNRS-UMR 7615 and Université Paris-6, École Supérieure de Physique et de Chimie Industrielles, 10, rue Vanquelin, F-75231 Paris cedex 05, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">D.</namePart><namePart type="family">Mills</namePart><affiliation>European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany</affiliation><affiliation>∗∗ Present address: Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Straße 7, 60528 Frankfurt-am-Main, Germany.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Haider</namePart><affiliation>European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany</affiliation><affiliation>∗∗∗ Present address: CEOS GmbH, hn Neuenheimer Feld 519, 69120 Heidelberg, Germany.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.L.</namePart><namePart type="family">Popot</namePart><affiliation>Correspondence and reprints.</affiliation><affiliation>CNRS-UPR 9052 and Université Paris-7, Institut de Biologie Physico-Chimique, 13, rue P-et-M-Curie, F-75005 Paris cedex 05, France</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">1998</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The composition and mass of complexes between Chlamydomonas reinhardtii cytochrome b6f and low molecular mass amphipathic polymers (‘amphipols’) have been studied using biochemical analysis and scanning transmission electron microscopy at liquid helium temperature (cryo-STEM). Cytochrome b6f was trapped by amphipols either under its native 14-meric state or as a delipidated, lighter form. A good consistency was observed between the masses of either form calculated from their biochemical composition and those determined by cryo-STEM. These data show that association with amphipols preserved the original aggregation state of the protein in detergent solution. Complexation with amphipols appears to facilitate preparation of the samples and mass determination by cryo-STEM as compared to conventional solubilization with detergents.</abstract><subject><genre>Keywords</genre><topic>membrane proteins</topic><topic>detergents</topic><topic>amphipols</topic><topic>electron microscopy</topic><topic>cytochrome b6f</topic></subject><subject><genre>Abbreviations</genre><topic>AmAc, ammonium acetate</topic><topic>AP, ammonium phosphate</topic><topic>cryo-STEM, scanning transmission electron microscopy at liquid helium temperature</topic><topic>cmc, critical micellar concentration</topic><topic>DPPC, dipalmitoylphosphatidylcholine</topic><topic>EM, electron microscopy</topic><topic>HG, 6-O-(N-heptylcarbamoyl)-methyl-α-D-glycopyranoside (Hecameg)</topic><topic>LM, dodecyl-β-D-maltoside (laurylmaltoside)</topic><topic>Mr, molecular mass</topic><topic>PC, phosphatidylcholine</topic><topic>SDS-PAGE, polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate</topic><topic>STEM, scanning transmission electron microscopy</topic><topic>TMV, tobacco mosaic virus</topic><topic>Tricine, N-tris (hydroxymethyl)methylglycine</topic></subject><relatedItem type="host"><titleInfo><title>Biochimie</title></titleInfo><titleInfo type="abbreviated"><title>BIOCHI</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">1998</dateIssued></originInfo><identifier type="ISSN">0300-9084</identifier><identifier type="PII">S0300-9084(00)X0056-9</identifier><part><date>1998</date><detail type="volume"><number>80</number><caption>vol.</caption></detail><detail type="issue"><number>5–6</number><caption>no.</caption></detail><extent unit="issue-pages"><start>354</start><end>571</end></extent><extent unit="pages"><start>475</start><end>482</end></extent></part></relatedItem><identifier type="istex">6C866A5375E3317494F2D755131C3F4F6729159B</identifier><identifier type="ark">ark:/67375/6H6-G4CKWCNR-H</identifier><identifier type="DOI">10.1016/S0300-9084(00)80014-0</identifier><identifier type="PII">S0300-9084(00)80014-0</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-G4CKWCNR-H/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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