An analytical expression for electron elastic scattering cross section from atoms and molecules in 1.0 keV to 1.0 MeV energy range

Yalçın, S.; Gürler, O.; Gultekin, A.; Gündoğdu, Ö.

doi:10.1016/j.physleta.2006.04.037

Cited by 12 publications

(13 citation statements)

References 20 publications

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“…The best fit to the data, with a R 2 value of 0.997, was a = 0.245, b = −1.665, and c = 2.81, plotted in Figure 5A together with the experimental data. This function can be used to estimate the critical exposure at 300 kV; the critical exposure at 200 kV can be expected to be about 25% lower ( Yalcin et al, 2006 ). The optimal exposure, plotted in Figure 5B , is ∼2.5 times the critical exposure ( Hayward and Glaeser, 1979 ).…”

Section: Resultsmentioning

confidence: 99%

Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6

Grant

Grigorieff

2015

eLife

808

672

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Biological specimens suffer radiation damage when imaged in an electron microscope, ultimately limiting the attainable resolution. At a given resolution, an optimal exposure can be defined that maximizes the signal-to-noise ratio in the image. Using a 2.6 Å resolution single particle cryo-EM reconstruction of rotavirus VP6, determined from movies recorded with a total exposure of 100 electrons/Å2, we obtained accurate measurements of optimal exposure values over a wide range of resolutions. At low and intermediate resolutions, our measured values are considerably higher than obtained previously for crystalline specimens, indicating that both images and movies should be collected with higher exposures than are generally used. We demonstrate a method of using our optimal exposure values to filter movie frames, yielding images with improved contrast that lead to higher resolution reconstructions. This ‘high-exposure’ technique should benefit cryo-EM work on all types of samples, especially those of relatively low-molecular mass.DOI: http://dx.doi.org/10.7554/eLife.06980.001

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Section: Resultsmentioning

confidence: 99%

Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6

Grant

Grigorieff

2015

eLife

808

672

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“…3 allows for selection of an exposure to maximize the SNR at any resolution. Although the amount of radiation damage per useful elastic interaction is not expected to change between 200 and 300 kV (Henderson, 1995), at 300 kV an exposure that is $25% higher would be required for the same number of elastic interactions to occur (Yalcin et al, 2006), resulting in higher critical and optimal exposures at that voltage.…”

Section: Resultsmentioning

confidence: 99%

“…This optimal exposure estimate assumes minimal detector and structural noise; for real samples and detectors, the optimal exposure is probably slightly lower. At 300 kV, 120 kV, and 100 kV, critical and optimal exposures would be $25% higher, $30% lower, and $40% lower, respectively (Henderson, 1995;Yalcin et al, 2006).…”

Section: Resultsmentioning

confidence: 99%

The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals

Baker

Smith

Bueler

et al. 2010

Journal of Structural Biology

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“…The mean free paths of both elastically and inelastically scattered electrons are significantly decreased at accelerating voltages of 200 kV and 100 kV compared to 300 kV (Yalcin et al, 2006;Angert et al, 1996;Yonekura et al, 2006), which is the highest voltage in the current high-end cryo-electron microscopes. Inelastically scattered electrons cause radiation damage to biological samples.…”

Section: Electron Energy and Energy Filteringmentioning

confidence: 96%

A new cryo-EM system for electron 3D crystallography by eEFD

Yonekura

Ishikawa

Maki-Yonekura

2019

Preprint

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A new cryo-EM system has been developed and investigated for use in protein electron 3D crystallography. The system provides parallel illumination of a coherent 300 kV electron beam to a sample, filters out energy-loss electrons through the sample with an in-column energy filter, and allows rotational data collection on a fast camera. It also possesses motorized cryo-sample loading and automated liquid-nitrogen filling for cooling of multiple samples. To facilitate its use, we developed GUI programs for efficient operation and accurate structure analysis. Here we report on the performance of the system and first results for thin 3D crystals of the protein complexes, catalase and membrane protein complex ExbBD. Data quality is remarkably improved with this approach, which we name eEFD (electron energy-filtered diffraction of 3D crystals), compared with those collected at 200 kV without energy filtration. Key advances include precise control of the microscope and recordings of lens fluctuations, which the programs process and respond to. We also discuss the merits of higher-energy electrons and filtration of energy-loss electrons in electron 3D crystallography.

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An analytical expression for electron elastic scattering cross section from atoms and molecules in 1.0 keV to 1.0 MeV energy range

Cited by 12 publications

References 20 publications

Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6

Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6

The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals

A new cryo-EM system for electron 3D crystallography by eEFD

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