Table 1.
Crystallographic data collection and refinement statistics for Scn/model ligand complex structures.
| Protein | human Scn | human Scn | human Scn | human Scn | human Scn |
| Mutations | C87S | C87S | C87S | C87S | C87S |
| Ligand | Fe-bisHA-CAM | Fe-tren(CAM)2 (1,2-HOPO) |
Fe-tren(CAM) (1,2-HOPO)2 |
Eu-tren(CAM) (1,2-HOPO)2 |
apo-ENT |
| Accession Code | 3HWE | 3HWF | 3HWG | 3TF6 | 3K3L |
| Space group | P41212 | P41212 | P41212 | P41212 | P41212 |
| Cell dimensions | |||||
| a = b, c (Å) | 115.43, 119.29 | 114.8, 118.35 | 114.08, 118.42 | 114.09, 118.19 | 114.20, 119.30 |
| α = β = γ (°) | 90 | 90 | 90 | 90 | 90 |
| Resolution (Å) | 50.0–2.80 (2.90–2.80) |
50.0–3.20 (3.28–3.20) |
50.0–2.19 (2.25–2.19) |
50.0–2.35 (2.41–2.35) |
50.0–2.62 (2.69–2.62) |
| Rmerge | 0.078 (0.24) | 0.135 (0.44) | 0.094 (0.43) | 0.068 (0.13) | 0.057 (0.41) |
| I/σ(I) | 12.6 (4.0) | 22.2 (6.26) | 24.3 (6.6) | 5.13 (4.10) | 50.3 (7.51) |
| Completeness (%) | 97.2 (96.0) | 99.7 (99.5) | 99.8 (100) | 99.6 (99.4) | 100 (99.9) |
| Redundancy | 5.5 (4.8) | 13.6 (13.7) | 10.5 (10.6) | 14.8 (2.3) | 12.9 (13.2) |
| Fe peak heights (σ) | 18, 14, 17 | 8, 7, 5 | 7, 17, 18 | NA | None observed |
| Rwork/Rfree | 0.230/0.283 | 0.218/0.265 | 0.242/0.268 | 0.192/0.214 | 0.260/0.307 |
| No. atoms | |||||
| Protein | 4062 | 3920 | 4008 | 4077 | 3682 |
| Heterogen | 198 | 159 | 239 | 77 | 128 |
| Waters | 84 | 17 | 167 | 117 | 116 |
| Wilson B (Å2) | 40.7 | 46.4 | 37.7 | 38.5 | 45.4 |
| Average B (Å2) | 34.0 | 31.0 | 31.1 | 38.0 | 47.0 |
| R.m.s. deviations | |||||
| Bond lengths (Å) | 0.006 | 0.016 | 0.005 | 0.016 | 0.005 |
| Bond angles (°) | 1.08 | 2.95 | 1.04 | 1.54 | 0.91 |
Values in parentheses are for the highest-resolution shell; NA: not applicable.