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Figure 1
Analysis of σA-weighted mFo − DFc, anomalous difference and the difference between anomalous difference maps in EFhd1 or EFhd2. (a) Schematic of mouse EFhd1 and human EFhd2. Each is composed of a PR (proline-rich) region, EF-hand 1 (EF1), EF-hand 2 (EF2), LM (ligand mimic) helix and CC (coiled-coil) region. Upper bars indicate the crystallized regions of EFhd1Ca, EFhd1Zn (residues, 79–180) and EFhd2Zn (residues, 82–180). (b), (c), (e) and (f) Overall structure of EFhd1Ca and EFhd1Zn. The EFhd1Ca is shown in lime green. The EFhd1Zn are shown in magenta, yellow, cyan or green. α1–6 indicates alpha helices 1–6. σA-weighted mFo − DFc (Fo − Fc) and anomalous difference maps are shown in cyan and magenta, respectively. (d) and (g) Overall structure of EFhd2Zn. The EFhd2Zn are shown in magenta, yellow, cyan or green. The Fo − Fc and anomalous difference maps are shown in cyan and magenta, respectively. (h) Difference between anomalous difference maps (ΔAno) calculated from the EFhd2Zn(P) and EFhd2Zn(R) datasets. The ΔAno map was represented in the EFhd2 structure and shown in gold. (i) Table showing the peak heights (σ) of anomalous difference and ΔAno maps calculated from the EFhd2Zn(P) and EFhd2Zn(R) datasets. All maps are contoured at 3.0σ.

IUCrJ
Volume 10| Part 2| March 2023| Pages 233-245
ISSN: 2052-2525
https://doi.org/10.1107/S2052252523001501