Table 1.
Data collection and refinement statistics
| Crystal | Rab7–RILP complex |
| Data collection | |
| Space group | P6522 |
| Unit cell dimension | |
| a/b/c (Å) | 93.13/93.13/132.83 |
| α/β/γ (deg) | 90.00/90.00/120.00 |
| Resolution range (Å) | 50–3.0 |
| Completeness (%) | 100 (100) |
| Unique reflections (N) | 7285 |
| Redundancy | 11.3 (11.4) |
| Rmerge (%)a | 9.7 (42.9) |
| I/σ | 6.6 (1.8) |
| Refinement | |
| Resolution (Å) | 20–3.0 |
| Used reflections (N) | 6904 |
| Total atoms (N) | 2082 |
| Protein atoms | 2015 |
| Nucleotide atoms | 32 |
| Mg2+ | 1 |
| Water molecules | 34 |
| Rwork (%)b | 26.8 (28.0) |
| Rfree (%)c | 27.8 (35.0) |
| R.m.s. deviation from ideal values | |
| Bond distance (Å) | 0.015 |
| Bond angle (deg) | 1.682 |
| Values in parentheses indicate the specific values in the highest resolution shell (3.1–3.0 Å). | |
| Rmerge=∑∣Ij−〈I〉∣/∑Ij, where Ij is the intensity of an individual reflection and 〈I〉 is the average intensity of that reflection. | |
| Rwork=∑∣∣Fo∣−∣Fc∣∣/∑∣Fc∣, where Fo denotes the observed structure-factor amplitude and Fc denotes the structure-factor amplitude calculated from the model. | |
| Rfree is as for Rwork but calculated with 5.0% of randomly chosen reflections omitted from the refinement. | |