Table S2.
HygX data collection and refinement statistics
| HygX-apo | HygX-Fe | HygX-AKG | HygX-AKG-hygB | HygX-AKG Ni-SAD | |
| Data collection | |||||
| PDB ID code | 4XC9 | 4ZPI | 4XCA | 4XCB | |
| Space group | P21212 | P212121 | P212121 | P212121 | P212121 |
| Cell dimensions | |||||
| a, b, c (Å) | 112.1, 274.4, 52.8 | 54.4, 109.0, 221.6 | 53.4, 112.0, 177.8 | 50.3, 117.5, 185.7 | 53.5, 112.1, 178.2 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Wavelength, Å | 0.979 | 1.739 | 0.979 | 0.979 | 1.485 |
| APS Beamline | 21-ID-F | 21-ID-D | 21-ID-F | 21-ID-F | 21-ID-D |
| Resolution, Å | 2.4 | 2.5 | 2.30 | 1.60 | 2.95 |
| Rsym, % | 8.0 (44.3) | 9.4 (58.4) | 7.1 (23.4) | 7.5 (44.6) | 10.5 (33.0) |
| I/σI | 14.7 (2.4) | 18.8 (2.2) | 21.1 (6.8) | 20.0 (3.3) | 27.3 (9.0) |
| Completeness, % | 92.9 (91.1) | 87.8 (89.8) | 96.1 (97.8) | 93.8 (92.8) | 99.5 (99.9) |
| Redundancy | 3.7 (3.6) | 3.7 (3.3) | 4.4 (4.4) | 4.9 (4.4) | 7.3 (7.5) |
| Refinement | |||||
| Resolution, Å | 2.4 | 2.5 | 2.3 | 1.6 | NA |
| No. of reflections | 61,588 | 149,043 | 46,643 | 126,897 | |
| Rwork/Rfree | 18.4/24.6 | 17.1/22.4 | 17.6/23.6 | 22.2/25.3 | |
| No. of atoms | |||||
| Protein | 11732 | 7851 | 7985 | 8160 | |
| Ligand/ion | 48 | 28 | 55 | 188 | |
| Water | 498 | 140 | 554 | 578 | |
| B-factors | |||||
| Protein | 40.7 | 39.5 | 30.6 | 22.2 | |
| Ligand/ion | 49.9 | 56.6 | 37.5 | 20.2 | |
| Water | 38.7 | 34.8 | 33.1 | 25.5 | |
| Ramachandran | |||||
| Favored, % | 96.7 | 96.7 | 97.6 | 97.8 | |
| Allowed, % | 3.2 | 3.3 | 2.3 | 2.2 | |
| Outliers, % | 0.1 | 0.0 | 0.1 | 0.0 | |
| rms deviations | |||||
| Bond lengths, Å | 0.008 | 0.008 | 0.008 | 0.006 | |
| Bond angles, ° | 1.12 | 1.11 | 1.09 | 1.07 |
All datasets were collected from a single crystal. Values in parentheses are for data in the highest-resolution shell. The HygX-AKG Ni-SAD dataset was used only for phasing. hygB, hygromycin B; NA, not applicable.