Table S1.
Statistics of crystallographic data collection and refinement
| Data processing | SOD1I35A |
| Space Group | P65 |
| Unit cell, Å | a, 70.82; b, 70.82; c, 70.01 |
| Unit cell, ° | α, 90.00; β, 90.00; γ, 120.00 |
| Wavelength, Å | 1.000 |
| Resolution range, Å | 46.1−3.60 (3.94−3.60) |
| Measured reflections | 11,303 (2,754) |
| Unique reflections | 2,203 (533) |
| Asymmetric unit contents | Dimer |
| Completeness, % | 92.8 (93.8) |
| Multiplicity | 5.1 (5.2) |
| Mean (I) half-set correlation CC(1/2) | 0.897 (0.572) |
| Rpim (all I+ and I−) | 0.162 (0.331) |
| Refinement statistics | |
| Resolution range, Å | 46.1−3.60 (4.53−3.60) |
| Rwork | 0.185 (0.189) |
| Rfree | 0.239 (0.236) |
| No. atoms, protein | 1,542 |
| rmsd bond lengths, Å | 0.004 |
| rmsd bond angles, ° | 0.780 |
| Mean B value, Å2 | 61.7 |
| Ramachandran plot | |
| Residues in most favored regions, % | 90.74 |
| Residues in allowed regions, % | 8.33 |
| Residues in disallowed regions, % | 0.93 |
Values in parentheses are for the highest-resolution shell. Rwork = Σ|Fobs|−|Fcalc|/ΣFobs, where Fcalc is the calculated protein structure factor from the atomic model (Rfree was calculated with 9.97% of the reflections selected).