Table 1. Data collection and statistics for anaerobic crystal structure resulting from the IPNS–AcβFV–Fe(II) complex.
| X-ray source | ID14–EH2, ESRF | |
|---|---|---|
| Wavelength λ (Å) | 0.934 | |
| Space group | P212121 | |
| Unit cell (a Å, b Å, c Å) | 46.23, 70.60, 100.64 | |
| Resolution shell (Å) | 21.98–1.30 | 1.37–1.30 |
| Number of reflections | 390499 | 44384 |
| Number of unique reflections | 80218 | 11381 |
| Average I/σI | 17.1 | 3.9 |
| Completeness (%) | 98.4 | 97.1 |
| Rmerge (%)* | 6.1 | 35.0 |
| Rcryst (%)† | 17.35 | |
| Rfree (%)‡ | 19.43 | |
| RMS deviation§ | 0.018 Å (1.916°) | |
| B factors (Å2)∥ | 10.3, 12.6, 19.8, 9.2, 25.3 | |
| Number of residues | 329 | |
| Number of water molecules | 355 |
* Rmerge=ΣjΣh|Ih,j−〈Ih〉|/ΣjΣh〈Ih〉×100.
† Rcryst=Σ||Fobs|−|Fcalc||/Σ|Fobs|×100.
‡ Rfree based on 4% of total reflections.
§ RMS deviation from ideality for bond lengths (followed by RMS deviation from ideality for bond angles).
∥ Average B factors in order: main chain, side chain, substrate, iron and solvent.