Table 1.
X-ray data collection and refinement statistics.
| Data collection | Apo | FMN-bound |
|---|---|---|
| Space group Unit-cell parameters | P21212 | P21212 |
| a, b, c (Å) | 132.494, 174.574, 85.345 | 131.616, 175.890, 84.934 |
| α, β, γ (°) | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 |
| Wavelength (Å) | 0.9870 | 0.9870 |
| Resolution (Å) | 50.00-2.20 (2.28-2.20) | 50-2.40 (2.49-2.40) |
| Unique reflections | 98498 (9746) | 78295 (7724) |
| Completeness (%) | 99.9 (100) | 99.9 (99.9) |
| Redundancy | 6.7 (6.5) | 6.8 (6.6) |
| I/σ(I) | 33.89 (4.72) | 29.07 (4.21) |
| Rmerge (%)a | 9.4 (57.0) | 10.5 (56.9) |
| Refinement | ||
| Rworking (%) | 17.47 | 18.11 |
| Rfree (%) | 21.30 | 22.11 |
| No. of | ||
| Protein residues | 1784 (homotetramer) | 1784 (homotetramer) |
| FMN | 4 | |
| solvent | 446 | 250 |
| R.m.s.d. from ideal geometry | ||
| Bond length (Å) | 0.007 | 0.010 |
| Bond angles (°) | 1.030 | 1.440 |
| Wilson B-value (Å2) | 33.48 | 36.17 |
| Average B-factors (Å2) | ||
| Protein | 41.27 | 48.79 |
| FMN | 47.44 | |
| Solvent | 40.10 | 45.04 |
| Ramachandran plot (%) | ||
| Favored | 96.85 | 97.40 |
| Allowed | 2.98 | 2.54 |
| Outliers | 0.17 | 0.06 |
aRmerge = ΣhklΣi|Ii(hkl)-<I(hkl)>|/ΣhklΣiIi(hkl). where <I(hkl)> is the mean intensity of multiply recorded reflections.
The coordinates and structure factors have been deposited in the Protein Data Bank with the accession code 5XKC (apo-BdsA) and 5XKD (FMN-bound).