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Machining protein microcrystals for structure determination by electron diffraction

We demonstrate that ion-beam milling of frozen, hydrated protein crystals to thin lamella preserves the crystal lattice to near-atomic resolution. This provides a vehicle for protein structure determination, bridging the crystal size gap between the nanometer scale of conventional electron diffracti...

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Detalles Bibliográficos
Autores principales: Duyvesteyn, Helen M. E., Kotecha, Abhay, Ginn, Helen M., Hecksel, Corey W., Beale, Emma V., de Haas, Felix, Evans, Gwyndaf, Zhang, Peijun, Chiu, Wah, Stuart, David I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6156647/
https://www.ncbi.nlm.nih.gov/pubmed/30171169
http://dx.doi.org/10.1073/pnas.1809978115
Descripción
Sumario:We demonstrate that ion-beam milling of frozen, hydrated protein crystals to thin lamella preserves the crystal lattice to near-atomic resolution. This provides a vehicle for protein structure determination, bridging the crystal size gap between the nanometer scale of conventional electron diffraction and micron scale of synchrotron microfocus beamlines. The demonstration that atomic information can be retained suggests that milling could provide such detail on sections cut from vitrified cells.