High-resolution structure determination by continuous-rotation data collection in MicroED

Nat Methods. 2014 Sep;11(9):927-930. doi: 10.1038/nmeth.3043. Epub 2014 Aug 3.


MicroED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroED called 'continuous rotation'. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroED in structural biology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Databases, Protein
  • Electrons
  • Imaging, Three-Dimensional / methods*
  • Information Storage and Retrieval / methods*
  • Lasers*
  • Microscopy, Video / methods*
  • Protein Conformation
  • Proteins / ultrastructure*
  • Rotation
  • Scattering, Small Angle
  • X-Ray Diffraction / methods*


  • Proteins