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Structural states of myelin observed by x-ray diffraction and freeze- fracture electron microscopy

Coordinated freeze-fracture electron microscopy and x-ray diffraction were used to visualize the morphological relation between compacted and native period membrane arrays in myelinated nerves treated with dimethylsulfoxide (DMSO). Comparison of x-ray diffraction at room temperature and at low tempe...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1979
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110425/
https://www.ncbi.nlm.nih.gov/pubmed/479295
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collection PubMed
description Coordinated freeze-fracture electron microscopy and x-ray diffraction were used to visualize the morphological relation between compacted and native period membrane arrays in myelinated nerves treated with dimethylsulfoxide (DMSO). Comparison of x-ray diffraction at room temperature and at low temperature was used as a critical measure of the extent of structural preservation. Our x-ray diffraction patterns show that in the presence of cryoprotective agents, it is possible to preserve with only small changes the myelin structure which exists at room temperature. These changes include a slight increase in packing disorder of the membrane, a small, negative thermal expansion of the membrane unit, and some reorganization in the cytoplasmic half of the bilayer. The freeze-fracture electron microscopy clearly demonstrates continuity of compact and native period phases in DMSO-treated myelin. Finally, the use of freezing to trap the transient, intermediate structure during a structural transition in glycerol is demonstrated.
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spelling pubmed-21104252008-05-01 Structural states of myelin observed by x-ray diffraction and freeze- fracture electron microscopy J Cell Biol Articles Coordinated freeze-fracture electron microscopy and x-ray diffraction were used to visualize the morphological relation between compacted and native period membrane arrays in myelinated nerves treated with dimethylsulfoxide (DMSO). Comparison of x-ray diffraction at room temperature and at low temperature was used as a critical measure of the extent of structural preservation. Our x-ray diffraction patterns show that in the presence of cryoprotective agents, it is possible to preserve with only small changes the myelin structure which exists at room temperature. These changes include a slight increase in packing disorder of the membrane, a small, negative thermal expansion of the membrane unit, and some reorganization in the cytoplasmic half of the bilayer. The freeze-fracture electron microscopy clearly demonstrates continuity of compact and native period phases in DMSO-treated myelin. Finally, the use of freezing to trap the transient, intermediate structure during a structural transition in glycerol is demonstrated. The Rockefeller University Press 1979-07-01 /pmc/articles/PMC2110425/ /pubmed/479295 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Structural states of myelin observed by x-ray diffraction and freeze- fracture electron microscopy
title Structural states of myelin observed by x-ray diffraction and freeze- fracture electron microscopy
title_full Structural states of myelin observed by x-ray diffraction and freeze- fracture electron microscopy
title_fullStr Structural states of myelin observed by x-ray diffraction and freeze- fracture electron microscopy
title_full_unstemmed Structural states of myelin observed by x-ray diffraction and freeze- fracture electron microscopy
title_short Structural states of myelin observed by x-ray diffraction and freeze- fracture electron microscopy
title_sort structural states of myelin observed by x-ray diffraction and freeze- fracture electron microscopy
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110425/
https://www.ncbi.nlm.nih.gov/pubmed/479295