Dark‐field electron microscopy of unstained biological materials embedded in Nanoplast
- 1 September 1987
- journal article
- Published by Wiley in Journal of Microscopy
- Vol. 147 (3) , 313-321
- https://doi.org/10.1111/j.1365-2818.1987.tb02842.x
Abstract
Extremely thin sections of unstained materials (beef liver catalase, double‐stranded calf thymus DNA, horse spleen ferritin and mammalian skeletal muscle), embedded in the water‐soluble melamine resin Nanoplast FB101, were studied by dark‐field electron microscopy and electron spectroscopic imaging.While ferritin molecules so recorded show 04 and 09 nm lattice fringes within the crystalline iron core, double‐stranded DNA shows a helical repeat with a spacing of 34 nm.The gain in resolution of structural detail reported here is probably due mainly to the reduced section thickness as compared to traditional thin‐sectioning techniques. As we reported earlier (Frösch & Westphal, 1984), melamine resins can be sectioned extremely thinly (<10 nm) and observed without a supporting film, making them especially suitable for dark‐field electron microscopy.Keywords
This publication has 15 references indexed in Scilit:
- Z‐Contrast in Biology A Comparison with Other Imaging ModesaAnnals of the New York Academy of Sciences, 1986
- Choosing the appropriate section thickness in the melamine embedding techniqueJournal of Microscopy, 1985
- Electron-phase-contrast imaging of unstained biological materials, embedded in a water-soluble melamine resinJournal of Ultrastructure Research, 1984
- Cryo-electron microscopy of virusesNature, 1984
- Electron microscopy of frozen biological suspensionsJournal of Microscopy, 1983
- High-resolution microanalysis of biological specimens by electron energy loss spectroscopy and by electron spectroscopic imagingJournal of Ultrastructure Research, 1980
- A simple method of optical filtrationUltramicroscopy, 1979
- The structure of mitochondrial membranes: A new conceptJournal of Ultrastructure Research, 1978
- Scanning transmission electron microscopy of unstained biological sectionsNature, 1978
- Electron Diffraction of Frozen, Hydrated Protein CrystalsScience, 1974