Table 2. Data collection and refinement statistics.
| SeMet-MilA L167M | MilA | MilA-CMP | MilA-dCMP | MilA-hmCMP | |
|---|---|---|---|---|---|
| Data collection | |||||
| Space group | P3221 | P3221 | P3221 | P3221 | P3221 |
| Unit cell parameters | |||||
| a, b, c (Å) | 107.7, 107.7, 112.1 | 107.8, 107.8, 112.0 | 109.6, 109.6, 113.4 | 109.3, 109.3, 113.2 | 109.3, 109.3, 112.8 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
| Resolution (Å) | 50–3.10 (3.21–3.10) | 50–2.20 (2.28–2.20) | 50–1.65 (1.71–1.65) | 50–2.10 (2.18–2.10) | 50–1.80 (1.86–1.80) |
| Rmerge (%) | 29.5 (63.6) | 15.6 (76.7) | 13.2 (88.5) | 11.8 (32.9) | 11.9 (73.6) |
| I/σI | 43.2 (19.4) | 23.2 (4.4) | 13.6 (1.9) | 17.8 (8.1) | 19.6 (3.7) |
| Completeness (%) | 100 (100) | 100 (100) | 96.6 (100) | 95.8 (100) | 100 (100) |
| Redundancy | 10.6 (10.9) | 21, 8 (19.0) | 6.7 (6.9) | 11.0 (11.3) | 11.2 (11.2) |
| Refinement | |||||
| Resolution (Å) | 48.02–2.20 | 48.73–1.65 | 49.26–2.10 | 49.24–1.80 | |
| Unique reflection | 38, 499 | 91, 516 | 43, 971 | 68, 810 | |
| Rwork/Rfree (%) | 16.8/20.7 | 17.2/19.4 | 15.5/20.6 | 18.7/20.8 | |
| Number of atoms | |||||
| Protein | 5,074 | 5,067 | 5,079 | 5,089 | |
| Ligand/ion | 0 | 42 | 40 | 46 | |
| Water | 336 | 547 | 501 | 201 | |
| B-factors (Å2) | |||||
| Overall | 27.32 | 24.55 | 21.6 | 19.7 | |
| Protein | 26.97 | 23.4 | 20.6 | 19.5 | |
| Ligand | N/A | 18.6 | 19.2 | 19.3 | |
| Water | 32.63 | 35.37 | 31.93 | 25.3 | |
| RMSD bond length (Å) | 0.008 | 0.006 | 0.007 | 0.005 | |
| RMSD bond angles (°) | 0.81 | 0.83 | 0.86 | 0.98 | |
Data for each structure were collected or calculated from a single crystal. RMSD, root-mean-square deviations from the ideal geometry. Data for the highest resolution shell are shown in parentheses.