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Merging of Image Data in Electron Crystallography

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Electron Crystallography of Soluble and Membrane Proteins

Abstract

Electron crystallography of membrane proteins uses cryo-transmission electron microscopy to record images and diffraction patterns of frozen-hydrated 2D crystals. Each two-dimensional (2D) crystal is only imaged once, at one specific tilt angle, and the recorded images can be automatically processed with the 2dx/MRC software package. Processed image data from non-tilted and tilted 2D crystals then need to be merged into a 3D reconstruction of the membrane protein structure. We here describe the process of the 3D merging, using the 2dx software system.

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Acknowledgments

This work was in part supported by the Swiss initiative for Systems Biology (SystemsX.ch, grant CINA), Swiss National Science Foundation (Grant 205321_126490), the NCCRs TransCure, Nano, and Structural Biology.

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Correspondence to Henning Stahlberg .

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Arheit, M., Castaño-Diéz, D., Thierry, R., Abeyrathne, P., Gipson, B.R., Stahlberg, H. (2013). Merging of Image Data in Electron Crystallography. In: Schmidt-Krey, I., Cheng, Y. (eds) Electron Crystallography of Soluble and Membrane Proteins. Methods in Molecular Biology, vol 955. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-176-9_11

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  • DOI: https://doi.org/10.1007/978-1-62703-176-9_11

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-175-2

  • Online ISBN: 978-1-62703-176-9

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