Table 1 Data collection and refinement statistics.
From: The FlhA linker mediates flagellar protein export switching during flagellar assembly
| Â | FlhAC(E351A/D356A) |
|---|---|
Data collection | |
Space group | P212121 |
Cell dimensions | |
 a, b, c (Å) | 71.7, 96.2, 114.1 |
 α, β, γ (°) | 90.0, 90.0, 90.0 |
Resolution (Å) | 73.5–2.80 (2.95–2.80)a |
Rmerge | 0.074 (0.317) |
CC(1/2) | 0.995 (0.915) |
I / σI | 8.1 (2.8) |
Completeness (%) | 97.1 (94.6) |
Redundancy | 3.4 (3.1) |
Refinement | |
Resolution (Å) | 73.5–2.80 (2.87–2.80) |
No. of reflections | 19,301 (1294) |
Rwork/Rfree | 23.2/29.0 (33.5/42.1) |
No. of atoms | |
 Protein | 5252 |
 Ligand/ion | 0 |
 Water | 0 |
B-factors | |
 Protein | 70.0 |
 Ligand/ion | – |
 Water | – |
R.m.s. deviations | Â |
 Bond lengths (Å) | 0.003 |
 Bond angles (°) | 0.680 |
