Journal
ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE CRYSTAL ENGINEERING AND MATERIALS
Volume 75, Issue -, Pages 523-531Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052520619009661
Keywords
electron diffraction; multislice calculation; inelastic electron scattering; protein crystallography; electron crystallography; cryo-EM
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Funding
- Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Forschung [5204.23000.160.02]
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Multi-slice simulations of electron diffraction by three-dimensional protein crystals have indicated that structure solution would be severely impeded by dynamical diffraction, especially when crystals are more than a few unit cells thick. In practice, however, dynamical diffraction turned out to be less of a problem than anticipated on the basis of these simulations. Here it is shown that two scattering phenomena, which are usually omitted from multi-slice simulations, reduce the dynamical effect: solvent scattering reduces the phase differences within the exit beam and inelastic scattering followed by elastic scattering results in diffusion of dynamical scattering out of Bragg peaks. Thus, these independent phenomena provide potential reasons for the apparent discrepancy between theory and practice in protein electron crystallography.
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