Zero‐loss energy‐filtered imaging of frozen‐hydrated proteins: model calculations and implications for future developments
- 1 June 1992
- journal article
- Published by Wiley in Journal of Microscopy
- Vol. 166 (3) , 389-400
- https://doi.org/10.1111/j.1365-2818.1992.tb01537.x
Abstract
SUMMARY: Energy‐filtered transmission electron microscopes operating in zero‐loss mode are used increasingly to study biological material in frozen‐hydrated conditions. The contrast enhancement and improved structural resolution obtainable by this method have been studied using Monte‐Carlo model calculations for the scattering processes occurring in such samples. Three models representing typical situations have been analysed, each normalized to minimal beam damage. It is shown that for proteins in thin layers of ice an optimal signal‐to‐noise ratio is achieved in the 80–120‐keV electron energy range. For proteins which have to be embedded in thicker ice layers, a considerably higher acceleration voltage is required. In particular, electron energies above 200 keV would be desirable for electron diffraction work on microcrystals.Keywords
This publication has 14 references indexed in Scilit:
- Cryosectioning of plant material frozen at high pressureJournal of Microscopy, 1991
- Radiation damage in dry and frozen hydrated organic materialJournal of Microscopy, 1991
- Zero-loss energy filtering as improved imaging mode in cryoelectronmicroscopy of frozen-hydrated specimensJournal of Structural Biology, 1990
- Cryo-electron microscopic studies of relaxed striated muscle thick filamentsJournal of Muscle Research and Cell Motility, 1990
- Cryo-electron microscopy of vitrified specimensQuarterly Reviews of Biophysics, 1988
- Cryoelectron Microscopy of Vitrified SpecimensPublished by Springer Nature ,1987
- Electron Beam Radiation Damage to Organic and Biological CryospecimensPublished by Springer Nature ,1987
- Electron scattering in ice and organic materialsJournal of Microscopy, 1982
- High-resolution microanalysis of biological specimens by electron energy loss spectroscopy and by electron spectroscopic imagingJournal of Ultrastructure Research, 1980
- Electron diffraction from single, fully-hydrated, ox-liver catalase microcrystalsActa Crystallographica Section A, 1975