Single particle refinement in electron crystallography: A pilot study.

Single particle refinement in electron crystallography: A pilot study. Research Abstract Details 

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Single particle refinement in electron crystallography: A pilot study. Abstract Text:

Philip J B Koeck,Pasi Purhonen,Ronny Alvang, Grundberg,Hans Hebert,

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 10A. 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.

Single particle refinement in electron crystallography: A pilot study. Publishing Authors By Initials

PJ Koeck,P Purhonen,R Alvang,B Grundberg,H Hebert,

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Single particle refinement in electron crystallography: A pilot study. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of structural biology

VOLUME: 160

Page Numbers: 344-52

Journal Abbreviation: J. Struct. Biol.

ISSN: 1047-8477

DAY: 11

MONTH: 09

YEAR: 2007

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LANGUAGE: eng

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AFFILIATION: Royal Institute of Technology, School of Technology and Health, Sweden; Södertörns Högskola, Department of Life Science, Sweden; Karolinska Institutet, Department of Bioscience at Novum, 141 57 Huddinge, Sweden.

Country: United States

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