Cryo-electron microscopy of vitreous sections
Identifieur interne : 000114 ( Ncbi/Curation ); précédent : 000113; suivant : 000115Cryo-electron microscopy of vitreous sections
Auteurs : Ashraf Al-Amoudi [Suisse] ; Jiin-Ju Chang [République populaire de Chine] ; Amélie Leforestier [France] ; Alasdair Mcdowall [Australie] ; Laurée Michel Salamin [Suisse] ; Lars P O. Norlén [Suisse] ; Karsten Richter [Allemagne] ; Nathalie Sartori Blanc [Suisse] ; Daniel Studer [Suisse] ; Jacques Dubochet [Suisse]Source :
- The EMBO Journal [ 0261-4189 ] ; 2004.
Abstract
Since the beginning of the 1980s, cryo-electron microscopy of a thin film of vitrified aqueous suspension has made it possible to observe biological particles in their native state, in the absence of the usual artefacts of dehydration and staining. Combined with 3-d reconstruction, it has become an important tool for structural molecular biology. Larger objects such as cells and tissues cannot generally be squeezed in a thin enough film. Cryo-electron microscopy of vitreous sections (CEMOVIS) provides then a solution. It requires vitrification of a sizable piece of biological material and cutting it into ultrathin sections, which are observed in the vitrified state. Each of these operations raises serious difficulties that have now been overcome. In general, the native state seen with CEMOVIS is very different from what has been seen before and it is seen in more detail. CEMOVIS will give its full potential when combined with computerized electron tomography for 3-d reconstruction.
Url:
DOI: 10.1038/sj.emboj.7600366
PubMed: 15318169
PubMed Central: 517607
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type="main">Cryo-electron microscopy of vitreous sections</title><author><name sortKey="Al Amoudi, Ashraf" sort="Al Amoudi, Ashraf" uniqKey="Al Amoudi A" first="Ashraf" last="Al-Amoudi">Ashraf Al-Amoudi</name><affiliation wicri:level="4"><nlm:aff id="O1">Laboratoire d'Analyse Ultrastructurale, Bâtiment de Biologie, Université de Lausanne, Lausanne, Switzerland</nlm:aff><country xml:lang="fr">Suisse</country><wicri:regionArea>Laboratoire d'Analyse Ultrastructurale, Bâtiment de Biologie, Université de Lausanne, Lausanne</wicri:regionArea><placeName><settlement type="city">Lausanne</settlement><region nuts="3" type="region">Canton de Vaud</region><settlement type="city">Lausanne</settlement></placeName><orgName type="university">Université de Lausanne</orgName></affiliation></author><author><name sortKey="Chang, Jiin Ju" sort="Chang, Jiin Ju" uniqKey="Chang J" first="Jiin-Ju" last="Chang">Jiin-Ju Chang</name><affiliation wicri:level="3"><nlm:aff id="O2">Institute of Biophysics, Academy of 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type="region">Canton de Vaud</region><settlement type="city">Lausanne</settlement></placeName><orgName type="university">Université de Lausanne</orgName></affiliation></author><author><name sortKey="Norlen, Lars P O" sort="Norlen, Lars P O" uniqKey="Norlen L" first="Lars P O" last="Norlén">Lars P O. Norlén</name><affiliation wicri:level="4"><nlm:aff id="O5">Groupe de Physique appliquée, Departement de physique, Université de Genève, Genève, Switzerland</nlm:aff><country xml:lang="fr">Suisse</country><wicri:regionArea>Groupe de Physique appliquée, Departement de physique, Université de Genève, Genève</wicri:regionArea><orgName type="university">Université de Genève</orgName><placeName><settlement type="city">Genève</settlement><region nuts="3" type="region">Canton de Genève</region></placeName></affiliation></author><author><name sortKey="Richter, Karsten" sort="Richter, Karsten" uniqKey="Richter K" first="Karsten" last="Richter">Karsten Richter</name><affiliation wicri:level="3"><nlm:aff id="O6">DKFZ, Molecular Genetics (B060), Heidelberg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>DKFZ, Molecular Genetics (B060), Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Blanc, Nathalie Sartori" sort="Blanc, Nathalie Sartori" uniqKey="Blanc N" first="Nathalie Sartori" last="Blanc">Nathalie Sartori Blanc</name><affiliation wicri:level="4"><nlm:aff id="O1">Laboratoire d'Analyse Ultrastructurale, Bâtiment de Biologie, Université de Lausanne, Lausanne, Switzerland</nlm:aff><country xml:lang="fr">Suisse</country><wicri:regionArea>Laboratoire d'Analyse Ultrastructurale, Bâtiment de Biologie, Université de Lausanne, Lausanne</wicri:regionArea><placeName><settlement type="city">Lausanne</settlement><region nuts="3" type="region">Canton de Vaud</region><settlement type="city">Lausanne</settlement></placeName><orgName type="university">Université de Lausanne</orgName></affiliation></author><author><name sortKey="Studer, Daniel" sort="Studer, Daniel" uniqKey="Studer D" first="Daniel" last="Studer">Daniel Studer</name><affiliation wicri:level="3"><nlm:aff id="O7">Anatomisches Institut, Postfach, Bern, Switzerland</nlm:aff><country xml:lang="fr">Suisse</country><wicri:regionArea>Anatomisches Institut, Postfach, Bern</wicri:regionArea><placeName><settlement type="city">Berne</settlement><region type="région" nuts="3">Canton de Berne</region></placeName></affiliation></author><author><name sortKey="Dubochet, Jacques" sort="Dubochet, Jacques" uniqKey="Dubochet J" first="Jacques" last="Dubochet">Jacques Dubochet</name><affiliation wicri:level="4"><nlm:aff id="O1">Laboratoire d'Analyse Ultrastructurale, Bâtiment de Biologie, Université de Lausanne, Lausanne, Switzerland</nlm:aff><country xml:lang="fr">Suisse</country><wicri:regionArea>Laboratoire d'Analyse Ultrastructurale, Bâtiment de Biologie, Université de Lausanne, Lausanne</wicri:regionArea><placeName><settlement type="city">Lausanne</settlement><region nuts="3" type="region">Canton de Vaud</region><settlement type="city">Lausanne</settlement></placeName><orgName type="university">Université de Lausanne</orgName></affiliation></author></analytic><series><title level="j">The EMBO Journal</title><idno type="ISSN">0261-4189</idno><idno type="eISSN">1460-2075</idno><imprint><date when="2004">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Since the beginning of the 1980s, cryo-electron microscopy of a thin film of vitrified aqueous suspension has made it possible to observe biological particles in their native state, in the absence of the usual artefacts of dehydration and staining. Combined with 3-d reconstruction, it has become an important tool for structural molecular biology. Larger objects such as cells and tissues cannot generally be squeezed in a thin enough film. Cryo-electron microscopy of vitreous sections (CEMOVIS) provides then a solution. It requires vitrification of a sizable piece of biological material and cutting it into ultrathin sections, which are observed in the vitrified state. Each of these operations raises serious difficulties that have now been overcome. In general, the native state seen with CEMOVIS is very different from what has been seen before and it is seen in more detail. CEMOVIS will give its full potential when combined with computerized electron tomography for 3-d reconstruction.</p></div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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