Table 1.
Data collection and refinement statistics
| OGAcryst (PDB 5TKE) | OGAcryst–thiamet-G (PDB 5UN9) | OGAcryst (D175N)–p53 (PDB 5UN8) | |
|---|---|---|---|
| Data collection | |||
| Space group | P21 | P21 | P21 |
| Cell dimensions | |||
| a, b, c (Å) | 82.0, 96.6, 89.3 | 82.5, 96.1, 89.5 | 89.9, 95.4, 149.3 |
| α, β, γ (°) | 90.0, 115.0, 90.0 | 90.0, 115.0, 90.0 | 90.0, 96.9, 90.0 |
| Resolution (Å) | 50.0–2.5 (2.59–2.50)a | 30.0–2.5 (2.54–2.50) | 50.0–2.1 (2.18–2.14) |
| Rmerge | 8.7 (72.2) | 6.3 (58.3) | 8.2 (72.0) |
| I/σ(I) | 19.5 (2.0) | 23.0 (2.1) | 18.4 (2.0) |
| CC1/2 | 99.9 (79.1) | 99.9 (78.5) | 99.8 (78.1) |
| Completeness (%) | 100.0 (100.0) | 99.5 (95.1) | 99.9 (100.0) |
| Redundancy | 6.4 (6.2) | 5.3 (5.2) | 4.9 (4.5) |
|
Refinement Resolution (Å) |
50.0–2.5 | 30.0–2.5 | 45.0–2.1 |
| No. reflections | 44,255 | 44,310 | 139,265 |
| Rwork / Rfree | 18.2 / 23.7 | 21.0 / 26.0 | 18.4 / 22.9 |
| No. atoms Protein |
6,921 | 6,922 | 14,015 |
| Ligand/peptide | 32 | 305 | |
| Water | 396 | 238 | 1,247 |
| B factors | 43.40 | 43.38 | 30.02 |
| Protein | 43.41 | 43.49 | 29.28 |
| Ligand/peptide | 29.73 | 29.07 | |
| Water | 42.68 | 40.93 | 38.56 |
| R.m.s. deviation Bond length (Å) |
0.008 | 0.011 | 0.009 |
| Bond angle (°) | 0.970 | 1.211 | 1.016 |
Each structure was determined from one crystal.
a
Values in parentheses are for highest-resolution shell.