Machining protein microcrystals for structure determination by electron diffraction
HME Duyvesteyn, A Kotecha… - Proceedings of the …, 2018 - National Acad Sciences
Proceedings of the National Academy of Sciences, 2018•National Acad Sciences
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.
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.
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.
National Acad Sciences
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