Most macromolecular structures are solved by X-ray diffraction using synchrotron light sources, but 30% of all protein crystals are too small (< 10 µm) for this. In 2013, Gonen’s group proposed a new approach called MicroED to collect complete 3D ED data from a submicron-sized 3D crystal of lysozyme to atomic resolution (2.6 Å).1,2 Independently, Zou’s group developed software-based rotation electron diffraction (RED) method,3 which is similar to MicroED. The RED method has shown to be very powerful and used for structure determination of > 80 inorganic and organic crystals.4,5 Högbom’s group has strong experience in protein crystallization, crystallography and structural analysis. We want to provide this 3D ED technique to the life science community by establishing a new national infrastructure facility.

The aim of the project is to establish a new SciLifeLab national infrastructure facility for 3D electron diffraction (ED) of macromolecular nano- and micron-sized crystals. The final goal is to build up an Electron Nanocrystallography service site within SciLifeLab for collection of high quality 3D electron diffraction data for structure determination of macromolecular crystals too small to be studied on synchrotron light sources.


Contact persons:

Prof. Xiaodong Zou, Department of Materials and Environmental Chemistry, SU


Tel: +46 8 16 23 89

Prof. Martin Högbom, Department of Biophysics and Biochemistry, SU



  • JEOL JEM 2100LaB6

  • JEOL JEM 2100F

  • Leica EM CPC Plunge Freezer

  • FEI Vitrobot Plunge Freezer

  • Gatan High-Tilt Cryo-Transfer Holder (914)


1 B. L. Nannenga, D. Shi, A. G. W. Leslie, T. Gonen, Nat. Methods 2014, 11, 927–930.

2 D. Shi, B. L. Nannenga, M. G. Iadanza, T. Gonen, eLife 2013, 2:e01345.

3 W. Wan, J. Sun, J. Su, S. Hovmöller, X. Zou, J. Appl. Crystallogr. 2013, 46, 1863–1873.

4 P. Guo, J. Shin, A. G. Greenaway, J. G. Min, J. Su, H. J. Choi, L. Liu, P. A. Cox, S. B. Hong, P. A. Wright, X. Zou, Nature 2015, 524, 74–78.

5 D. Feng, T.-F. Liu, J. Su, M. Bosch, Z. Wei, W. Wan, D. Yuan, Y.-P. Chen, X. Wang, K. Wang, X. Lian, Z.-Y. Gu, J. Park, X. Zou, H.-C. Zhou, Nat. Comm. 2015, 6, 5979.


Figure 1. Continuous Rotation Data Collection
Figure 1. Continuous rotation data collection.



Movie 1. Continuous rotation data collection of lysozyme.


Figure 2. Single electron diffraction pattern taken from lysozyme
Figure 2. Single electron diffraction pattern taken from lysozyme.


Figure 3. 2.6 Å Lysozyme structure solved from electron diffraction data
Figure 3. 2.6 Å lysozyme structure solved from electron diffraction data.


Figure 4. Negative stained high resolution TEM image showing the packing of the lysozyme crystal.

Figure 4. Negative stained high resolution TEM image showing the packing of the lysozyme crystal.