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Updated: Jul 30, 2026

Crystallization of Membrane Proteins in Lipidic Mesophases
Published on: March 28, 2011
Crystallization of an AMPA receptor binding domain without agonist: importance of carbohydrate content and
J Féthière1, A Andersson, K Keinänen
1Ion Channel Structure Research Group, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany.
Abstract:
An AMPA-specific ionotropic glutamate receptor binding domain was overexpressed using the baculovirus system and purified by immunoaffinity and metal-affinity chromatography. Purified protein was enzymatically deglycosylated. Both glycosylated and deglycosylated proteins crystallized under the same conditions and in the same space group (P2). In both cases, it was observed that the use of MPD as a cryoprotectant induced a significant reduction in the unit-cell volume compared with glycerol or sucrose. For crystals of deglycosylated protein, cryoprotection with MPD also yielded a dramatic improvement in resolution.
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