Table 1.
Data collection and structure refinement statistics
| CesT/Re-CsrA | |
|---|---|
| Data collection a | |
| Space group | C2 |
| Cell dimensions | |
| a, b, c (Å) | 252.8, 52.6, 93.4 |
| α, β, γ (°) | 90.0, 96.7, 90.0 |
| Wavelength (Å) | 0.97775 |
| Resolution (Å) | 50–2.3 (2.38–2.30) |
| R merge | 0.072 (1.308) |
| R pim | 0.030 (0.557) |
| CC1/2 | 0.997 (0.877) |
| I/sigI | 23.0 (1.25) |
| Completeness (%) | 99.8 (99.8) |
| Redundancy | 6.7 (6.5) |
| Refinement | |
| Resolution (Å) | 49.35–2.30 |
| No. reflections | 54651 |
| Completeness (%) | 98.8 |
| Rwork/Rfree | 0.233/0.251 |
| No. atoms | |
| Protein | 7830 |
| Ligand/ion | 0 |
| Water | 138 |
| B-factors | |
| Protein | 87.03 |
| Ligand/ion | |
| Water | 67.49 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.003 |
| Bond angles (°) | 0.579 |
| Ramachandran plot (%) | |
| Favored region | 96.40 |
| Allowed region | 3.60 |
| Outlier region | 0 |
Values in parentheses are for the highest-resolution shell
a A single crystal was used to collect the data