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The Power of Freeze-Fracture Technique in Electron Microscopy

Published online by Cambridge University Press:  02 July 2020

B. Papahadjopoulos-Sternberg
B. Papahadjopoulos-Sternberg*
Affiliation:
Dept. of Microbiology, School of Dentistry, University of the Pacific, San Francisco, CA94115
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Abstract

In the early 1960s, concerns about artifacts in preparing biological material for electron microscopy led to a new technique whereby samples are rapidly frozen, fractured under high vacuum, the fractured surfaces shadowed and replicated with a thin metal-carbon coat, and the cleaned replica examined in a transmission electron microscope. Pioneered by Moor and Muhlethaler subcellular structures are revealed with extraordinary three-dimensional clarity at near-molecular resolution. Furthermore, it was observed and proven at model systems as well as biological membranes that lipid bilayers split along their hydrophobic interior during freeze-fracture procedure. Therefore, freeze-fracture electron microscopy (FFEM) has the unique advantage of accessing the hydrophobic interior of biological (FIG.l, 5 and 6) as well as artificial bilayers (FIG. 2, 4, 5, and 6). Here it permits study of pattern generated by intrinsic proteins as well as lipids (FIG. 1 and 2).

Type
Recent Techniques for the Fixation and Staining of Biological Samples (Organized by M. Sanders and K. McDonald)
Information
Microscopy and Microanalysis , Volume 7 , Issue S2: Proceedings: Microscopy & Microanalysis 2001, Microscopy Society of America 59th Annual Meeting, Microbeam Analysis Society 35th Annual Meeting, Long Beach, California August 5-9, 2001 , August 2001 , pp. 1212 - 1213
Copyright
Copyright © Microscopy Society of America 2001

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References

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