Table 1.
Crystallographic table
| Protein | JSiR1 |
| Data collection | |
| Space group | I 121 |
| Cell dimensions | |
| a, b, c (Å) | 50.95, 130.63, 77.30 |
| α, β, γ (°) | 90, 100.55, 90 |
| Resolution (Å) | 46.78–2.145 (2.39–2.145) |
| Ellipsoidal high-resolution limit | 2.1, 2.3, 2.6 |
| Rmerge | 0.142 (4.12) |
| Rpim | 0.092 (0.693) |
| CC1/2 | 0.995 (0.537) |
| I/Sigma | 7.2 (1.4) |
| Completeness (%) | 70.5 (12.9) (spherical) 90.6 (51.7) (ellipsoidal) |
| Multiplicity | 6.1 (3.5) |
| Refinement | |
| Resolution (Å) | 46.78–2.145 |
| No. reflections | 18,977 |
| Rwork/Rfree | 0.215/0.255 |
| No. atoms | |
| Protein | 2,417 |
| Ligand/ion | 20 (9-cis retinal)/133 (OLC) |
| Water | 54 |
| B-factors | |
| Protein | 38.5 |
| Ligand/ion | 36.46 (9-cis retinal)/51.7 (OLC) |
| Water | 39.75 |
| R.M.S. deviations | |
| Bond lengths (Å) | 0.008 |
| Bond angles (°) | 1.010 |
| Ramachandran favored | 97.7% |
| Ramachandran accepted | 2.3% |
| Ramachandran outliers | 0% |