Electron diffraction and three-dimensional crystallography for structural biology

Clabbers, Max T. B. and Abrahams, Jan Pieter. (2018) Electron diffraction and three-dimensional crystallography for structural biology. CRYSTALLOGRAPHY REVIEWS, 24 (3). pp. 176-204.

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Electron crystallography is increasingly becoming a viable alternative for structure elucidation of three-dimensional, multi-nanometre sized crystals of beam-sensitive organics and macromolecules. Because electrons interact with matter strongly, crystals cannot be much more than 200nm thick. Diffracted volumes are therefore small, leading to a poor signal-to-noise ratio (SNR) as beam damage limits the total electron dose. Data can be collected in diffraction - and imaging mode. Imaging has the advantage of providing spatial phase information but comes at a substantial cost in SNR. Highly sensitive hybrid pixel detectors push the limits of high-quality diffraction data acquisition even further. Data integration, structure solution and refinement are feasible with existing software after minor adaptations. We review the current state of electron diffraction for structural biology, including instrumentation, data acquisition and structure determination.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Further Journal Contribution
Note:Publication type according to Uni Basel Research Database: Journal item
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Last Modified:28 Mar 2020 14:15
Deposited On:28 Mar 2020 14:07

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