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Machining protein microcrystals for structure determination by electron diffraction

DOI: 10.1073/pnas.1809978115 DOI Help

Authors: Helen M. E. Duyvesteyn (University of Oxford; Diamond Light Source) , Abhay Kotecha (University of Oxford; Thermo Fisher Scientific) , Helen M. Ginn (University of Oxford; Diamond Light Source,) , Corey W. Hecksel (Diamond Light Source) , Emma V. Beale (Diamond Light Source) , Felix De Haas (Thermo Fisher Scientific) , Gwyndaf Evans (Diamond Light Source) , Peijun Zhang (Diamond Light Source; University of Oxford) , Wah Chiu (Stanford University; SSRL SLAC National Accelerator Laboratory) , David I. Stuart (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Proceedings Of The National Academy Of Sciences , VOL 74

State: Published (Approved)
Published: August 2018

Open Access Open Access

Abstract: 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.

Journal Keywords: electron crystallography; FIB; protein crystal; diffraction; structure

Subject Areas: Technique Development, Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Talos-Talos Arctica at Diamond

Documents:
1809978115.full.pdf