期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 115, 期 38, 页码 9569-9573出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1809978115
关键词
electron crystallography; FIB; protein crystal; diffraction; structure
资金
- Wellcome [ALR00750-B500.1, ALR00040, 101122/Z/13/Z, 206422/Z/17/Z, 090532/Z/09/Z]
- UK Medical Research Council (MRC) [MR/N00065X/1]
- NIH [P41GM103832]
- Wellcome
- MRC
- Biotechnology and Biological Sciences Research Council
- BBSRC [BB/S003339/1] Funding Source: UKRI
- MRC [MR/N00065X/1] Funding Source: UKRI
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据