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- W2912721216 abstract "Electron DiffractionProtein crystallographers who hope to use x-ray diffraction to determine structures have long struggled with growing large, uniform protein crystals. Crystals only a few micrometers thin are ideal for diffraction by electrons but are likewise hard to grow predictably. Focused ion beam milling can create thin slices from large protein crystals that are ideal for electron diffraction. Martynowycz et al. demonstrate that continuous rotation of a single crystal section with careful control of electron dose can yield a high-resolution structure of a model protein. Such a strategy should be generally applicable to otherwise intractable microcrystals, which are, as of now, a common dead end.Structure 10.1016/j.str.2018.12.003 (2019)." @default.
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- W2912721216 date "2019-02-14" @default.
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- W2912721216 title "Microsolution for macromolecules" @default.
- W2912721216 doi "https://doi.org/10.1126/science.363.6428.704-f" @default.
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