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Journal Article

Crystallization of an AMPA receptor binding domain without agonist: importance of carbohydrate content and flash-cooling conditions

MPS-Authors
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Féthière,  James
Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society;

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Andersson,  Arnold
Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94176

Madden,  Dean R.
Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society;

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http://journals.iucr.org/d/issues/2000/12/00/gr2069/gr2069.pdf
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http://dx.doi.org/10.1107/S0907444900014104
(Any fulltext)

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Citation

Féthière, J., Andersson, A., Keinänen, K., & Madden, D. R. (2000). Crystallization of an AMPA receptor binding domain without agonist: importance of carbohydrate content and flash-cooling conditions. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), 56, 1625-1629. doi:10.1107/S0907444900014104.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-33EF-E
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.