Table I.
X-Ray Data Collection, Analysis, and Refinement Statistics for the Crystal Structure of the RpfE
| Data collection | |
| Space group | P21 |
| Cell dimensions | |
| a, b, c (Å) | 34.54 84.00 72.63 |
| α, β, γ (°) | 90, 103.53, 90 |
| Wavelength | 1.11 |
| Resolution (Å) | 42.0–2.756 (2.85–2.76) |
| No. reflections | 10,478 (1021) |
| Rmerge (%) | 12.9% (81.9) |
| I/σI | 109.5/10.2 (13.9/6.9) |
| Completeness (%) | 99.61 (96.32) |
| Redundancy | 3.9 (3.8) |
| Refinement | |
| Resolution (Å) | 36.0–2.76 |
| Rwork/Rfree | 0.235/0.287 |
| No. atoms | 3241 |
| Protein | 3234 |
| Water | 7 |
| Protein residues | 431 |
| B-factors | 49.30 |
| Protein | 49.30 |
| Water | 44.90 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.002 |
| Bond angles (°) | 0.58 |
| Ramachandran plot | |
| Ramachandran favored (%) | 93 |
| Ramachandran outliers (%) | 1.7 |
| PDB ID | 4CGE |