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November 19, 2013SHILAP Revista de lepidopterologíaOpen Access

Three-dimensional electron crystallography of protein microcrystals

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Authors

DSDan ShiBNBrent L. NannengaMIM.G. Iadanza

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Overview

Methodological study demonstrates high-resolution protein structure determination from 3D microcrystals using electron diffraction, highlighting MicroED as a viable structural biology tool.

Key Points

  • To determine whether high-resolution three-dimensional protein structures can be solved from microcrystals using electron cryo-microscopy diffraction methods.
  • Lysozyme microcrystals were flash-frozen on electron microscopy grids and examined under an electron cryo-microscope.
  • A tilt-series electron diffraction protocol collected up to 90 patterns per crystal with 0.1–1° tilt increments and an accumulated electron dose under 10 e⁻/Ų.
  • Diffraction data from three individual crystals were indexed, merged, and phased using molecular replacement followed by crystallographic refinement.
  • Electron diffraction patterns yielded measurable reflections extending to 1.7 Å resolution.
  • Merged diffraction data from three microcrystals enabled complete structure determination and refinement of lysozyme to 2.9 Å resolution.

Cite This Study

Shi et al. (2013) studied this question.

synapsesocial.com/papers/69dd2bb0fb7610310c100eabhttps://doi.org/10.7554/elife.01345
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