Table 1. Data collection and refinement statistics.
| X-ray diffraction data | ||
| Unit Cell | a: | 107.25 Å |
| b: | 107.25 Å | |
| c: | 128.25 Å | |
| α: | 90.0° | |
| β: | 90.0° | |
| γ: | 120.0° | |
| Space group: | P6322 | |
| Resolution: | 2.2 Å | |
| Number of unique reflections: | 22919 | |
| Completeness: | 99.9% | |
| R-merge1: | 0.155 | |
| I/sig(I): | 7.7 | |
| Redundancy: | 24.5 | |
| Structure refinement | ||
| R-work2: | 0.240 | |
| R-free: | 0.273 | |
| Number of reflections | R-work: | 19964 |
| R-free: | 807 | |
| Number of atoms refined | Protein: | 2745 |
| Co-factor: | 62 | |
| Ion: | 1 | |
| Water molecules: | 84 | |
| Overall B-value: | 17.9 Å2 | |
| Root mean square deviations | Bond length: | 0.007 Å |
| Bond angle: | 1.3° |
1
Rsym = ΣhΣi|Ii(h)−<I(h)>|/ΣhΣi |Ii(h)|, where Ii(h) is the intensity measurement for a reflection h and <I(h)> is the mean intensity for this reflection.
2
R-value = Σi∥Fi,obs|−k|Fi,cal∥/Σi|Fi,obs|.