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Machining protein microcrystals for structure determination by electron diffraction
DOI:10.1073/pnas.1809978115.png)
摘要
En 中文
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.
Keyword:
electron crystallography
FIB
protein crystal
diffraction
structure
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期刊
P
IF:
9.1
论文数:
10.8W
被引数:
73.5W
机构
引用论文
First lasing and operation of an angstrom-wavelength free-electron laser埃波长自由电子激光器的首次激光发射和操作
NATURE PHOTONICS
IF32.9

