Table 3.
Data collection and refinement statistics (molecular replacement)
| ATP-PRT/TIHa | ATP-PRT/TIH | ATP-PRT/l-His | |
|---|---|---|---|
| Data collection | |||
| Space group | H 3 2 (155) | H 3 2 (155) | H 3 2 (155) |
| Cell dimensions | |||
| a, b, c (Å) | 115.48, 115.48, 124.60 | 117.51, 117.51, 127.36 | 117.01, 117.01, 127.33 |
| α, β, γ (°) | 90.00, 90.00, 120.00 | 90,00, 90.00, 120.00 | 90.00, 90.00, 120.00 |
| Resolution (Å) | 46.41–1.76 | 47.25–2.06 | 42.44–2.02 |
| (1.79–1.76)b | (2.12–2.06)b | (2.07–2.02)b | |
| R sym or R merge | 0.033 (0.828) | 0.041 (0.690) | 0.033 (0.714) |
| I/σI | 20.6(1.0) | 16.1(2.0) | 22.3(2.1) |
| Completeness (%) | 99.8 (98.2) | 99.7 (99.9) | 99.7 (100) |
| Redundancy | 5.2 (3.6) | 4.6 (4.8) | 4.8 (5.1) |
| Refinement | |||
| Resolution (Å) | 47.25–2.06 | 42.44–2.02 | |
| (2.12–2.06) | (2.07–2.02) | ||
| No. reflections | 20989 | 22067 | |
| R work / R free | 0.1975/0.2307 | 0.1979/0.2378 | |
| No. atoms | 2274 | 2284 | |
| Protein | 2166 | 2161 | |
| Ligand/ion | 26 | 36 | |
| Water | 82 | 87 | |
| B-factors | |||
| Protein | 50.56 | 48.83 | |
| Ligand/ion | 74.67 | 77.01 | |
| Water | 52.47 | 52.90 | |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.004 | 0.007 | |
| Bond angles (°) | 0.64 | 0.86 | |
aData set used for anomalous scattering difference map calculation
bNumber of crystals was one for each structure. Values in parentheses are for highest-resolution shell