Structure of the ATP-Synthase from Chloroplasts and Mitochondria Studied by Electron Microscopy

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dc.contributor.authorBoekema, Egbert J.
dc.contributor.authorSchmidt, Günter
dc.contributor.authorGräber, Peter
dc.contributor.authorBerden, Jan A.
dc.date.accessioned2019-01-02T09:33:52Z
dc.date.available2019-01-02T09:33:52Z
dc.date.issued1988
dc.description.abstractThe structure of the ATP-synthase, F0F1 , from spinach chloroplasts and beef heart mitochondria has been investigated by electron microscopy with negatively stained specimens. The detergent-solubilized ATP-synthase forms string-like structures in which the F0 parts are aggregated. In most cases, the F, parts are arranged at alternating sides along the string. The F0 part has an approximate cylindrical shape with heights of 8.3 and 8.9 nm and diameters of 6.2 and 6.4 nm for the chloroplast and mitochondrial enzyme, respectively. The F, parts are disk-like structures with a diameter of about 11.5 nm and a height of about 8.5 nm. The F, parts are attached to the strings, composed of Fn parts, in most cases, with their smallest dimension parallel to the strings. The stalk connecting F0 and F, has a length of 3.7 nm and 4.3 nm and a diameter of 2.7 nm and 4.3 nm for the chloroplast and mitochondrial enzyme, respectively.en
dc.identifier.eissn1865-7125
dc.identifier.issn0939-5075
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/8753
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-7882
dc.language.isoen
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/3.0/
dc.subject.ddc570 Biowissenschaften; Biologiede
dc.subject.otherATP-synthaseen
dc.subject.otherenzyme structureen
dc.subject.otherelectron microscopyen
dc.titleStructure of the ATP-Synthase from Chloroplasts and Mitochondria Studied by Electron Microscopyen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1515/znc-1988-3-412
dcterms.bibliographicCitation.issue3-4
dcterms.bibliographicCitation.journaltitleZeitschrift für Naturforschung Cde
dcterms.bibliographicCitation.originalpublishernameDe Gruyteren
dcterms.bibliographicCitation.originalpublisherplaceBerlin
dcterms.bibliographicCitation.pageend225
dcterms.bibliographicCitation.pagestart219
dcterms.bibliographicCitation.volume43
tub.accessrights.dnbfree
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Physikalische Chemie / Biophysikalische Chemiede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.groupFG Physikalische Chemie / Biophysikalische Chemiede
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlinde

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