Table I. Details of data collection and refinement.
| FadR–myristoyl-CoA | FadR–operator | |
|---|---|---|
| Spacegroup | P6122 | P6122 |
| Unit cell (Å) | a = 59.48 | a = 93.00 |
| b = 59.48 | b = 93.00 | |
| c = 290.48 | c = 334.83 | |
| Resolution, last bin (Å) | 30–2.1 (2.18–2.1) | 25–3.25 (3.37–3.25) |
| Unique reflections | 18 556 | 14 138 |
| Redundancy | 4.7 (4.9) | 6.2 (4.5) |
| Completeness (%) | 97.8 (95.5) | 98.0 (98.6) |
| Rmerge | 0.038 (0.292) | 0.143 (0.458) |
| I/σI | 17.9 (5.1) | 6.6 (2.5) |
| Rcryst | 0.226 | 0.271 |
| Rfree | 0.256 | 0.309 |
| No. of atoms | 1781 protein | 3631 protein + 2 Au + 3 Cl |
| 134 water | 28 water | |
| 63 ligand | 773 DNA | |
| Wilson B-factor (Å2) | 39.4 | n.d. |
| <B> protein (Å2) | 42.5 | 67.8 |
| <B> DNA (Å2) | – | 61.8 |
| <B> (adenosine + pyrophosphate) | 65.9 | – |
| <B> (pantetheine + myristate) | 48.8 | – |
| <B> (water) | 50.5 | 35.2 |
| R.m.s.ds from ideal geometry | ||
| bond lengths (Å) | 0.009 | 0.013 |
| bond angles (°) | 1.46 | 1.7 |
| main chain B-factors (Å2) | 1.7 | 1.1 |
Data were collected at 100 K (λ = 0.92 Å for FadR–myristoyl-CoA and λ = 1.025 Å for the FadR–operator complex). All measured data were included in the refinement.