期刊
STRUCTURE
卷 26, 期 6, 页码 848-+出版社
CELL PRESS
DOI: 10.1016/j.str.2018.04.004
关键词
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资金
- Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD [ZIA BC 010826, ZIA BC 010278, ZIA BC 010825, ZIA BC 010827]
- NATIONAL CANCER INSTITUTE [ZIABC010278, ZIABC010412, ZIABC010825, ZIABC010826, ZIABC010827] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [ZIAHL001027] Funding Source: NIH RePORTER
The advent of direct electron detectors has enabled the routine use of single-particle cryo-electron microscopy (EM) approaches to determine structures of a variety of protein complexes at near-atomic resolution. Here, we report the development of methods to account for local variations in defocus and beaminduced drift, and the implementation of a datadriven dose compensation scheme that significantly improves the extraction of high-resolution information recorded during exposure of the specimen to the electron beam. These advances enable determination of a cryo-EM density map for beta-galactosidase bound to the inhibitor phenylethyl beta-D-thiogalactopyranoside where the ordered regions are resolved at a level of detail seen in X-ray maps at similar to 1.5 angstrom resolution. Using this density map in conjunction with constrained molecular dynamics simulations provides a measure of the local flexibility of the noncovalently bound inhibitor and offers further opportunities for structure-guided inhibitor design.
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