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research article

The 2DX robot: a membrane protein 2D crystallization Swiss Army knife

Iacovache, Ioan  
•
Biasini, Marco
•
Kowal, Julia
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2010
Journal of structural biology

Among the state-of-the-art techniques that provide experimental information at atomic scale for membrane proteins, electron crystallography, atomic force microscopy and solid state NMR make use of two-dimensional crystals. We present a cyclodextrin-driven method for detergent removal implemented in a fully automated robot. The kinetics of the reconstitution processes is precisely controlled, because the detergent complexation by cyclodextrin is of stoichiometric nature. The method requires smaller volumes and lower protein concentrations than established 2D crystallization methods, making it possible to explore more conditions with the same amount of protein. The method yielded highly ordered 2D crystals diffracting to high resolution from the pore-forming toxin Aeromonas hydrophila aerolysin (2.9A), the plant aquaporin SoPIP2;1 (3.1A) and the human aquaporin-8 (hAQP8; 3.3A). This new method outperforms traditional 2D crystallization approaches in terms of accuracy, flexibility, throughput, and allows the usage of detergents having low critical micelle concentration (CMC), which stabilize the structure of membrane proteins in solution.

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Type
research article
DOI
10.1016/j.jsb.2009.12.001
Web of Science ID

WOS:000275296100013

PubMed ID

19963066

Author(s)
Iacovache, Ioan  
Biasini, Marco
Kowal, Julia
Kukulski, Wanda
Chami, Mohamed
van der Goot, F Gisou  
Engel, Andreas
Rémigy, Hervé-W.
Date Issued

2010

Publisher

Elsevier

Published in
Journal of structural biology
Volume

169

Issue

3

Start page

370

End page

8

Subjects

2D crystallization

•

Membrane protein

•

Cyclodextrin

•

High throughput

•

Electron microscopy

•

2-Dimensional Crystallization

•

Electron Crystallography

•

Angstrom Structure

•

Bio-Beads

•

Reconstitution

•

Solubilization

•

Resolution

•

Aerolysin

•

Channel

•

Phase

Editorial or Peer reviewed

NON-REVIEWED

Written at

EPFL

EPFL units
VDG  
Available on Infoscience
December 10, 2009
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/44751
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