Table 3. Iron-Bound EntC and Irp9 Data Collection and Refinement Statistics.
| Fe-EntC | Fe-Irp9 | |
|---|---|---|
| Data Collectiona | ||
| wavelength (Å) | 1.739 | 1.739 |
| space group | P41212 | P21 |
| cell dimensions | ||
| a (Å) | 81.38 | 56.39 |
| b (Å) | 81.38 | 145.35 |
| c (Å) | 262.28 | 58.44 |
| β (deg) | – | 108.02 |
| resolution (Å) | 38.86–2.94 (3.12–2.94) | 39.12–2.16 (2.23–2.16) |
| Rsymb | 0.167 (0.754) | 0.096 (0.729) |
| Rpim | 0.044 (0.204) | 0.039 (0.355) |
| total observations | 541745 (82062) | 641609 (33764) |
| total unique observations | 19603 (3001) | 47172 (3604) |
| mean (I/σ(I)) | 21.6 (5.6) | 18.3 (3.0) |
| completeness (%) | 99.4 (96.7) | 98.9 (88.1) |
| redundancy | 27.6 (27.3) | 13.6 (9.4) |
| anomalous completeness (%) | 99.4 (96.5) | 98.0 (79.3) |
| anomalous redundancy | 15.2 (14.6) | 6.8 (5.0) |
| DelAnom correlation between half-setsc | 0.128 (−0.017) | –0.056 (0.014) |
| mid-slope of anom normal probabilityd | 1.039 | 0.945 |
| Refinement | ||
| resolution (Å) | 38.86–2.94 (3.02–2.94) | 36.52–2.16 (2.21–2.16) |
| Rcryste | 18.00 (22.88) | 17.20 (22.47) |
| Rfree | 26.67 (37.91) | 23.48 (29.15) |
| total unique observations | 19521 (1152) | 47138 (2205) |
| no. of non-hydrogen atoms | ||
| protein | 5663 | 6419 |
| ligand | 32 | 17 |
| metal | 4 | 2 |
| water | 0 | 155 |
| bond rmsd (Å) | 0.03 | 0.013 |
| angle rmsd (deg) | 1.471 | 1.214 |
| overall mean B factor (Å2) | 47.68 | 29.16 |
| Ramachandran plot analysisf | ||
| most favored regions | 93.24 | 95.57 |
| additionally allowed regions | 6.48 | 4.31 |
| disallowed regions | 0.28 | 0.12 |
a
Data were indexed and scaled with XDS.
b
Rsym = ∑h|Ih – ⟨I⟩|/∑hIh, where Ih is the intensity of reflection h and ⟨I⟩ is the mean intensity of all symmetry-related reflections.
c
Anomalous correlation between half-sets = ∑||FPH ± FP| – FHcalc|/∑|FPH| reported for all centric reflections.
d
Mid-slope of anomalous probability = ⟨|FH|/||FP + FH| – |FPH||⟩ reported for all reflections.
e
Rcryst = ∑||Fo| – |Fc||/∑|Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes. Five percent of the relections were reserved for the calculation of Rfree.
f
Calculated with MolProbity.