Table 1.
Statistics of data collection and refinement
| DapF-bound RppH | |
|---|---|
| Number of crystals | 1 |
| Space group | P41212 |
| Cell dimensions | |
| a, b, c (Å) | 86.42, 86.42, 173.09 |
| α, β, γ (o) | 90, 90, 90 |
| Number of molecules in ASU | 1 |
| Wavelength (Å) | 0.9792 |
| Resolution (Å) | 45–2.30 (2.38–2.30) |
| R merge (%) | 9.8 (121.7) |
| R pim (%) | 3.9 (47.6) |
| I/σI σ | 18.8 (2.4) |
| Completeness (%) | 99.8 (99.8) |
| Number of measured reflections | 418 998 |
| Number of unique reflections | 30 026 |
| Redundancy | 14 (13.9) |
| Wilson B factor (Å2) | 46.4 |
| R work/Rfree (%) | 20.6/23.9 |
| Number of atoms | 3454 |
| Protein | 3355 |
| Main chain | 1696 |
| Side chain | 1659 |
| Water | 79 |
| Other entities | 22 |
| Average B value (Å2) | 65.2 |
| Protein | 65.3 |
| main chain | 63.6 |
| side chain | 67.1 |
| Water | 56.3 |
| Other entities | 72.2 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.009 |
| Bond angle (°) | 1.030 |
| Ramachandran plot statistics (%) | |
| Most favorable | 89.4 |
| Allowed | 10.6 |
| Disallowed | 0 |
The highest-resolution shell is shown in parentheses. Values in parentheses indicate the highest resolution shell. Rmerge=ΣhΣi|Ih,i-Ih|/ΣhΣiIh,i, where Ih is the mean intensity of the i observations of symmetry-related reflections of h. R=Σ|Fobs-Fcalc|/ΣFobs, where Fcalc is the calculated protein structure factor from the atomic model (Rfree is calculated with 5% of the reflections selected).