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 possiÂ 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 meaningÂ 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
Annual Review of Biophysics – Annual Reviews
Published: Jun 1, 1981
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