Low Temperature Electron Microscopy

Low Temperature Electron Microscopy In the investigation of biological ultrastructure by electron microscopy the most significant observation to date is a membrane of Halobacterium halobium (73). nm repeat in the purple With a high degree of certainty, the spacing can be ascribed to the inter a-helical separation within bacteriorhodopsin molecules. This resolution is only made possi­ ble because of the unique properties of the purple membrane and is due in particular to its two-dimensional crystallinity, which results in a repetition of the structural data. For a nonperiodic object, the meaning­ ful resolution often lies between ribosomes and 5 nm, as illustrated by comparing two models that have been proposed independently for the structure of (45, 82). More frequently, it is in even larger structures that uncertainties become apparent. For example, there are good arguments for questioning the validity of the unit membrane as it is seen in most ultrathin sections settle the question of whether chromatin fibres are (62), and electron microscopy has not yet been able to 10, 20 or 30 nm in diameter. In short, the resolution obtained with biological structures is disappointing when compared with the resolving power of modern electron microscopes of between 0.2 and 0.5 nm. It http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Biophysics Annual Reviews

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Publisher
Annual Reviews
Copyright
Copyright 1981 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
1936-122X
eISSN
1936-1238
DOI
10.1146/annurev.bb.10.060181.001025
pmid
7020572
Publisher site
See Article on Publisher Site

Abstract

In the investigation of biological ultrastructure by electron microscopy the most significant observation to date is a membrane of Halobacterium halobium (73). nm repeat in the purple With a high degree of certainty, the spacing can be ascribed to the inter a-helical separation within bacteriorhodopsin molecules. This resolution is only made possi­ ble because of the unique properties of the purple membrane and is due in particular to its two-dimensional crystallinity, which results in a repetition of the structural data. For a nonperiodic object, the meaning­ ful resolution often lies between ribosomes and 5 nm, as illustrated by comparing two models that have been proposed independently for the structure of (45, 82). More frequently, it is in even larger structures that uncertainties become apparent. For example, there are good arguments for questioning the validity of the unit membrane as it is seen in most ultrathin sections settle the question of whether chromatin fibres are (62), and electron microscopy has not yet been able to 10, 20 or 30 nm in diameter. In short, the resolution obtained with biological structures is disappointing when compared with the resolving power of modern electron microscopes of between 0.2 and 0.5 nm. It

Journal

Annual Review of BiophysicsAnnual Reviews

Published: Jun 1, 1981

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