Table 1. Data collection and structure refinement statistics.
| Data set | Crystal form A | Crystal form B |
| Data collection statistics | ||
| Beam line | ID14-4, ESRF | ID14-1, ESRF |
| Wavelength (Å) | 0.9762 | 0.9334 |
| Resolution (Å) | 58.38–2.23 (2.35–2.23) | 50.11–2.10 (2.16–2.10) |
| Space group | C2 | P61 |
| Cell parameters a/b/c (Å) | 153.7, 154.3, 64.5 | 88.7, 88.7, 100.2 |
| α/β/γ (°) | 90.0, 102.3, 90.0 | 90.0, 90.0, 120.0 |
| Unique reflections | 69794 (9862) | 26203 (2179) |
| Redundancy | 3.0 (2.6) | 7.6 (7.6) |
| I/σ | 3.8 (1.6) | 13.1 (2.9) |
| Completeness (%) | 98.2 (95.7) | 100.0 (100.0) |
| Rmerge | 0.215 (0.686) | 0.109 (0.666) |
| Rpim | 0.143 (0.507) | 0.064 (0.390) |
| Wilson B factor (Å2) | 20.0 | 21.6 |
| Refinement statistics | ||
| Data range (Å) | 54.33–2.23 (2.29–2.23) | 44.39–2.10 (2.16–2.10) |
| Used reflections | 66255 | 24851 |
| Rwork | 0.222 (0.348) | 0.180 (0.272) |
| Rfree | 0.258 (0.367) | 0.236 (0.320) |
| No of monomers/ASU | 4 | 1 |
| No. of protein atoms | 10580 | 2732 |
| No. of FAD molecules | 4 | 1 |
| No. of NADP+ molecules | 4 | 1 |
| No. of water molecules | 340 | 164 |
| No. of K+ | 4 | - |
| Average B-factors (Å2) | ||
| Protein | 33.1 | 42.5 |
| FAD | 14.8 | 25.4 |
| NADP+ | 25.2 | 30.0 |
| Water molecules | 27.1 | 41.0 |
| K+ ions | 19.0 | - |
| R.m.s. deviations | ||
| Rmsd bond length (Å) | 0.014 | 0.019 |
| Rmsd bond angles (°) | 1.700 | 2.125 |
| Ramachandran plot (% residues) | ||
| Allowed | 1319 (98.1%) | 322 (95.8%) |
| Generously allowed | 25 (1.9%) | 13 (3.9%) |
| Disallowed | 0 (0.0%) | 1 (0.3%) |
Values in parentheses are for the highest-resolution shell, ASU: Asymmetric unit.