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3D reconstruction of two-dimensional crystals
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 3342888
Author(s) Stahlberg, Henning; Biyani, Nikhil; Engel, Andreas
Author(s) at UniBasel Stahlberg, Henning
Year 2015
Title 3D reconstruction of two-dimensional crystals
Journal Archives of Biochemistry and Biophysics
Volume 581
Pages / Article-Number 68-77
Abstract Electron crystallography of two-dimensional (2D) crystals determines the structure of membrane proteins in the lipid bilayer by imaging with cryo-electron microscopy and image processing. Membrane proteins can be packed in regular 2D arrays by their reconstitution in the presence of lipids at low lipid to protein weight-to-weight ratio. The crystal quality depends on the protein purity and homogeneity, its stability, and on the crystallization conditions. A 2D crystal presents the membrane protein in a functional and fully lipidated state. Electron crystallography determines the 3D structure even of small membrane proteins up to atomic resolution, but 3D density maps have a better resolution in the membrane plane than in the vertical direction. This problem can be partly eliminated by applying an iterative algorithm that exploits additional known constraints about the 2D crystal. 2D electron crystallography is particularly attractive for the structural analysis of membrane proteins that are too small for single particle analyses and too unstable to form 3D crystals. With the recent introduction of direct electron detector cameras, the routine determination of the atomic 3D structure of membrane-embedded membrane proteins is in reach.
Publisher Elsevier Academic Press
ISSN/ISBN 0003-9861
edoc-URL http://edoc.unibas.ch/40164/
Full Text on edoc No
Digital Object Identifier DOI 10.1016/j.abb.2015.06.006
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/26093179
ISI-Number WOS:000360187700009
Document type (ISI) Journal Article, Review
 
   

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