Table 2. Crystallographic data and refinement statistics.
| Semet 6H7V |
Apo 6HCP |
Complex 6H7F |
|
|---|---|---|---|
| Data collection | |||
| Space group | C 1 2 1 | C 1 2 1 | C 1 2 1 |
| Cell dimensions | |||
|
a, b, c (Å) α, β, γ (°) |
182.3, 220.4, 101.7 90, 98.7, 90 |
180.2, 219.5, 101.4 90, 99.2, 90 |
179.6, 220.7, 101.1 90, 99.2, 90 |
| Resolution (Å) | 139.53–2.54 (2.61–2.54)* | 57.24–1.83 (1.88–1.83)* | 49.93–2.26 (2.30–2.26) |
| Rsym or Rmerge | 0.12 (0.789) | 0.049 (0.665) | 0.108 (0.844) |
| I / σI | 19.3 (3.8) | 17.1 (2.2) | 9.2 (1.6) |
| Completeness (%) | (99.9) 100 | 99.7 (99.6) | 99.8 (99.9) |
| Redundancy | 15.2 (14.1) | 3.8 (3.9) | 3.8 (3.8) |
| CC half | - | - | 0.995 (0.527) |
| Anom completeness | 99.9 (99.9) | - | - |
| Ano multiplicity | 7.5 (6.9) | - | - |
| Refinement | |||
| Resolution (Å) | 139.53–2.54 | 57.24–1.83 | 49.93–2.26 |
| No. of reflections | 123,580 | 322,409 | 171,799 |
| Rwork/Rfree | 0.183/0.213 | 0.156/0.176 | 0.187/0.217 |
| No. of atoms | |||
| Protein | 15,424 | 16,060 | 15,854 |
| Ligand/ion | 201 | 754 | 691 |
| Water | 303 | 1995 | 752 |
| B-factors | |||
| Protein | 44.4 | 33.40 | 39.70 |
| Ligand/ion | 60.4 | 57.70 | 59.22 |
| Water | 36.90 | 45.90 | 36.87 |
| R.m.s deviations | |||
| Bond lengths (Å) | 0.010 | 0.008 | 0.008 |
| Bond angles (°) | 1.24 | 1.16 | 0.958 |
Each dataset was collected from a single crystal. *Values in parentheses are for highest-resolution shell.