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Single particle refinement in electron crystallography: A pilot study
KTH, School of Technology and Health (STH), Structural Biotechnology.
KTH, School of Technology and Health (STH).
KTH, School of Technology and Health (STH), Structural Biotechnology.
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2007 (English)In: Journal of Structural Biology, ISSN 1047-8477, E-ISSN 1095-8657, Vol. 160, no 3, 344-352 p.Article in journal (Refereed) Published
Abstract [en]

Electron crystallography can be used to determine the structures of membrane proteins at near-atomic resolution in some cases. However, most electron crystallography projects remain at a resolution around 10 angstrom. This might be partly due to lack of flatness of many two-dimensional crystals. We have investigated this problem and suggest single particle processing of locally averaged unit cells to improve the quality and possibly the resolution of three-dimensional maps. Applying this method to the secondary transporter melibiose permease we have calculated a three-dimensional map that is clearer and easier to interpret than the map derived using purely electron-crystallographic methods.

Place, publisher, year, edition, pages
2007. Vol. 160, no 3, 344-352 p.
Keyword [en]
electron crystallography, single particle reconstruction, membrane proteins, crystal distortion
National Category
Biological Sciences
URN: urn:nbn:se:kth:diva-24889DOI: 10.1016/j.jsb.2007.09.001ISI: 000251473500010OAI: diva2:353879

QC 20100929

Available from: 2010-09-29 Created: 2010-09-29 Last updated: 2013-07-19Bibliographically approved

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Köck, Philip J. B.Grundberg, BjörnHebert, Hans
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