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Figure 1
Comparison of electron density maps (2Fo − Fc, contour level σ = 1.5) of lysozyme in the original structure (PDB entry 4et8; 1.90 Å yellow mesh and model) and the reprocessed data using all frames (1.49 Å, blue mesh and model). (a) and (b) Active-site residue Asp52 could be modeled with an alternative conformation using the reprocessed data. (c) and (d) Another section of the structure around Tyr23 with the same maps as described above (but with contour level σ = 0.8) shows more detailed density for the aromatic amino acids when using the reprocessed data.

IUCrJ
Volume 11| Part 2| March 2024| Pages 190-201
ISSN: 2052-2525
https://doi.org/10.1107/S205225252400054X