Table 2. Data collection and refinement statistics.
| PP5 apo | PP5 + P5SA-2 | |
|---|---|---|
| Crystal parameters | ||
| Space group | P41212 | P41212 |
| Cell constants | a=b=50.1 Å, c=379.2 Å | a=b=51.1 Å, c=365.7 Å |
| Molecules per AU* | 1 | 1 |
| Data collection | ||
| Beamline | SLS, PXI–X06SA | SLS, PXI–X06SA |
| Wavelength (Å) | 1.0 | 1.0 |
| Resolution range (Å)† | 40–2.3 (2.4–2.3) | 30–2.0 (2.1–2.0) |
| Number of observed reflections | 140950 | 286970 |
| Number of unique reflections‡ | 22932 | 34075 |
| Completeness (%)† | 99.5 (99.9) | 98.5 (93.1) |
| Rmerge (%)†§ | 4.1 (53.7) | 3.8 (43.5) |
| I/σ (I)† | 22.3 (4.4) | 28.8 (5.6) |
| Refinement (REFMAC5) | ||
| Resolution range (Å) | 15–2.3 | 15–2.0 |
| Number of atoms | ||
| Protein | 3757 | 3749 |
| Water | 63 | 106 |
| Rwork/Rfree (%)║ | 23.8/27.1 | 21.4/26.1 |
| RMSDs¶ | ||
| Bond lengths/angles (Å)/(°) | 0.005/0.99 | 0.015/1.68 |
| Average B-factor (Å2) | 74.1 | 51.0 |
| Ramachandran plot (%)** | 95.2/4.6/0.2 | 95.7/4.3/0 |
| PDB accession code | 4JA9 | 4JA7 |
*Asymmetric unit.
†The values in parentheses of resolution range, completeness, Rmerge and I/σ (I) correspond to the last resolution shell.
‡Friedel pairs were treated as identical reflections.
§Rmerge (I)=ΣhklΣj |I(hkl)j–<Ihkl>|/ΣhklΣjI(hkl)j where I(hkl)j is the jth measurement of the intensity of reflection hkl and <I(hkl)> is the average intensity.
║
R=Σhkl | |Fobs| − |Fcalc| |/Σhkl |Fobs|, where Rfree is calculated without a sigma cut-off for a randomly chosen 5% of reflections, which were not used for structure refinement and Rwork is calculated for the remaining reflections.
¶Deviations from ideal bond lengths/angles.
**Number of residues in favoured region/allowed region/outlier region.