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Single particle refinement in electron crystallography: A pilot study
Södertörns högskola, Institutionen för livsvetenskaper. KTH / Karoliska institutet.
Vise andre og tillknytning
2007 (engelsk)Inngår i: Journal of Structural Biology, ISSN 1047-8477, E-ISSN 1095-8657, Vol. 160, nr 3, s. 344-352Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2007. Vol. 160, nr 3, s. 344-352
Emneord [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
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Identifikatorer
URN: urn:nbn:se:sh:diva-22889DOI: 10.1016/j.jsb.2007.09.001ISI: 000251473500010PubMedID: 17936013Scopus ID: 2-s2.0-36048997627OAI: oai:DiVA.org:sh-22889DiVA, id: diva2:711636
Tilgjengelig fra: 2014-04-10 Laget: 2014-03-28 Sist oppdatert: 2017-12-05bibliografisk kontrollert

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Koeck, Philip J. B.

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