TABLE 1.
Data collection and refinement statistics
Each structure was determined using diffraction data by one crystal.
| Rv08051–318 | 5′-AMP-Rv08051–318 | |
|---|---|---|
| Data collection | ||
| Space group | P41212 | P41212 |
| Cell dimensions | ||
| a, b, c (Å) | 100.18, 100.18, 80.25 | 100.40, 100.40, 80.80 |
| Resolution (Å) | 50-1.60 (1.64-1.60)a | 50-1.80 (1.84-1.80) |
| Rmerge | 5.7 (52.8) | 6.7 (61.9) |
| I/σI | 34.9 (2.3) | 29.5 (3.7) |
| Completeness (%) | 99.9 (99.6) | 99.9 (100.0) |
| Redundancy | 9.4 (5.0) | 8.0 (7.7) |
| Refinement | ||
| Resolution (Å) | 32.4-1.6 (1.64-1.60)a | 31.8-1.8 (1.85-1.80) |
| No. reflections (F > 0σ) | 54,293 | 38,804 |
| Rwork/Rfree | 15.9/17.7 (31.1/33.1) | 15.0/16.8 (20.4/25.7) |
| No. atomsb | ||
| Protein | 2,229 | 2,229 |
| Ligand/ion | ||
| Iron | 1 | 1 |
| Manganese | 1 | 1 |
| Bis-Tris | 14 | 14 |
| 5′-AMP (active site) | 23 | |
| Acetate (active site) | 4 | |
| MPD | 16 (2 molecules) | 24 (3 molecules) |
| Acetate | 4 | 4 |
| Water | 292 | 247 |
| B-factors | ||
| Protein | 24.3 | 26.5 |
| Ligand/ion | ||
| Iron | 14.3 | 17.0 |
| Manganese | 14.4 | 16.7 |
| Bis-Tris | 20.7 | 23.9 |
| 5′-AMP (active site) | 29.2 | |
| Acetate (active site) | 16.1 | |
| MPD | 42.1 | 55.9 |
| Acetate | 54.9 | 64.7 |
| Water | 33.9 | 34.8 |
| Wilson B-factor | 26.6 | 29.1 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.008 | 0.009 |
| Bond angles (°) | 1.16 | 1.24 |
a Values in parentheses are for highest-resolution shell.
b Values for asymmetric unit, containing one monomer of the dimer. The dimer is generated using symmetry operation Y, X, −Z.