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Single particle refinement in electron crystallography: A pilot study
Södertörn University, School of Life Sciences. KTH / Karoliska institutet.
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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 Å. 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]
Crystal distortion, Electron crystallography, Membrane proteins, Single particle reconstruction, melibiose, membrane protein, permease, article, calculation, crystal structure, crystallography, elementary particle, measurement, pilot study, priority journal, protein structure, structure analysis, three dimensional imaging, Computer Simulation, Crystallization, Escherichia coli Proteins, Fourier Analysis, Imaging, Three-Dimensional, Microscopy, Electron, Transmission, Models, Molecular, Pilot Projects, Protein Conformation, Symporters
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:sh:diva-22889DOI: 10.1016/j.jsb.2007.09.001ISI: 000251473500010PubMedID: 17936013ScopusID: 2-s2.0-36048997627OAI: diva2:711636
Available from: 2014-04-10 Created: 2014-03-28 Last updated: 2014-04-10Bibliographically approved

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Koeck, Philip J. B.
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