Two-Dimensional Crystallisation of Membrane Proteins and Structural Assessment

Fotiadis, Dimitrios José; Engel, Andreas (2015). Two-Dimensional Crystallisation of Membrane Proteins and Structural Assessment. In: eLS (pp. 1-10). John Wiley & Sons, Ltd.

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Two-dimensional (2D) crystallisation of Membrane proteins reconstitutes them into their native environment, the lipid bilayer. Electron crystallography allows the structural analysis of these regular protein–lipid arrays up to atomic resolution. The crystal quality depends on the protein purity, ist stability and on the crystallisation conditions. The basics of 2D crystallisation and different recent advances are reviewed and electron crystallography approaches summarised. Progress in 2D crystallisation, sample preparation, image detectors and automation of the data acquisition and processing pipeline makes 2D electron crystallography particularly attractive for the structural analysis of membrane proteins that are too small for single-particle analyses and too unstable to form three-dimensional (3D) crystals.

Item Type:

Book Section (Encyclopedia Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Fotiadis, Dimitrios José

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health

ISBN:

9780470015902

Publisher:

John Wiley & Sons, Ltd.

Language:

English

Submitter:

Barbara Järmann-Bangerter

Date Deposited:

01 Mar 2016 14:44

Last Modified:

19 Sep 2017 19:04

BORIS DOI:

10.7892/boris.76090

URI:

https://boris.unibe.ch/id/eprint/76090

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