Comparing serial X-ray crystallography and microcrystal electron diffraction (MicroED) as methods for routine structure determination from small macromolecular crystals

Wolff, A.M.; Young, I.D.; Sierra, R.G.; Brewster, A.S.; Martynowycz, M.W.; Nango, E.; Sugahara, M.; Nakane, T.; Ito, K.; Aquila, A.; Bhowmick, A.; Biel, J.T.; Carbajo, S.; Cohen, A.E.; Cortez, S.; Gonzalez, A.; Hino, T.; Im, D.; Koralek, J.D.; Kubo, M.; Lazarou, T.S.; Nomura, T.; Owada, S.; Samelson, A.J.; Tanaka, T.; Tanaka, R.; Thompson, E.M.; van den Bedem, H.; Woldeyes, R.A.; Yumoto, F.; Zhao, W.; Tono, K.; Boutet, S.; Iwata, S.; Gonen, T.; Sauter, N.K.; Fraser, J.S.; Thompson, M.C.

doi:10.1107/S205225252000072X

Figure 6
Visualization of the 2mF_o − F_c map and the refined model measured from an FIB-milled crystal using MicroED. The conformation of residues coupled to the catalytic site resembles structures previously solved under cryogenic conditions using X-ray crystallography (PDB entry 3k0m). For some regions of the structure, the cryogenic X-ray and MicroED structures are indistinguishable. A previously published multi-conformer model produced from data acquired at room temperature is provided for comparison (PDB entry 3k0n). Following refinement, ensembles were generated using phenix.ensemble_refine. In the right panel, a histogram of the χ₁ angles for residue 113 is plotted for the ensemble. All members of the ensemble adopted the same rotameric position as previous cryogenic structures.

IUCrJ

Volume 7| Part 2| March 2020| Pages 306-323

ISSN: 2052-2525

https://doi.org/10.1107/S205225252000072X

BIOLOGY | MEDICINE

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