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Figure 3
Structure of ccNiR. (a) The room-temperature structure is shown in light pink and the electron-density map is shown in transparent light blue. The ten heme cofactors are shown in salmon and the Ca ions are shown in bright green. (b) Close-up view of one of the heme cofactors. The heme(s) as well as the side chains in (a) are well resolved even at a resolution of 3.3 Å. (c) Comparison of the SSX structure (green) with the previously published Laue structure (blue). The unit cell of the SSX structure is larger by 5 Å in one of the axes. Another difference is the presence of a PEG molecule in the SSX structure, which is marked by dotted squares. (d) Close-up view of the asymmetric unit of ccNiR. The omit difference map is shown at ±3σ. The PEG molecule traverses the entire width of the unit cell. Only ten PEG oxyethylene monomers can be modeled in the asymmetric unit, while the rest are generated by crystallographic symmetry.

IUCrJ
Volume 12| Part 1| January 2025|
ISSN: 2052-2525
https://doi.org/10.1107/S2052252524010868