Table 1.
X-ray statistics
| Data collection | PPase:Pi2 | PPase:FPPi |
|---|---|---|
| Rmerge (I) (last shell) | 7.5% (36.3%) | 8.1% (24.7%) |
| Resolution | 8.0–1.15 Å | 8.0–1.9 Å |
| Independent observations (multiplicity) | 212 495 (3.6) | 53 366 (4.5) |
| Completeness (last shell) | 85.4% (75.5%) | 97.6% (92.6%) |
| I/σI (last shell) | 11.95 (3.0) | 12.58 (4.9) |
| Refinement | ||
| Reflections |F| > 2 σ (F) | 87 817 | |
| Reflections I (I > 4σ I) | 205 805 (154 122) | |
| Rwork/Rfree (F > 4σ F) | 13.6% (11.0%) | 15.5/18.2% |
| Non H atoms | 5769 | 5261 |
| Multiple conformations | 202 (3.5%) | 106 (2.0%) |
| Waters | 1021 | 648 |
| Protein B-factors | 13.8 Å2 | 9.4 Å2 |
| Phosphate B-factors | 8.8 Å2 | 9.0 Å2 |
| Mn2+ B-factors | 8.7 Å2 | 7.8 Å2 |
| rmsd from target values | ||
| Bond lengths | 0.011 Å | 0.007 Å |
| Bond angles | 0.026 Å | 1.5° |
| Rigid-bond ADPs | 0.05 Å2 | |
| Approximate isotropic ADPs | 0.108 Å2 |
Rmerge = Σ | Ih − 〈I〉 |/Σ Ih, where Ih is the measured and 〈I〉 the average intensity of reflection hkl. Rfree (7) and Rwork are conventional crystallographic R-factors (R = Σ ∥ Fobs | − | Fcalc ∥/Σ | Fobs |), where Fobs is the observed and Fcalc the calculated structure factor of reflection hkl. B-factors were analyzed with moleman (G. Kleywegt, unpublished program) and values for rms deviations are from shelxpro for PPase:Pi2 and CNS for PPase:FPPi. ADP, anisotropic displacement parameter.