Table 1.
Data collection and refinement statistics.
| T. thermophilus ribosome–Plazomicin | AAC(2′)-Ia–CoA–Acetylated Plazomicin | |
|---|---|---|
| Data collection | ||
| Space group | P 21 21 21 | P 32 2 1 |
| Cell dimensions | ||
| a, b, c (Å) | 209.5, 449.4, 619.6 | 73.5, 73.5 147.1 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 120 |
| Resolution (Å) | 127.5–3.27 (3.38–3.27)a | 58.43–1.95 (2.02–1.95) |
| Rmerge | 0.214 (1.27) | 0.052 (0.96) |
| I/σI | 5.94 (1.2) | 18.9 (2.1) |
| Completeness (%) | 99.7 (97.5) | 98.8 (97.5) |
| Redundancy | 6.5 (5.4) | 8.1 (7.0) |
| Refinement | ||
| Total no. of reflections | 5,816,392 (463,077) | 273,465 (23,176) |
| Rwork/Rfree | 0.214/0.277 | 0.192/0.225 |
| No. of atoms | 296,449 | 3096 |
| Macromolecules | 294,983 | 2756 |
| Ligand/ion | 1464 | 224 |
| Water | 2 | 116 |
| B-factors | 86.8 | 48.9 |
| Macromolecules | 87.0 | 46.9 |
| Ligand/ion | 61.7 | 58.0 |
| Water | 56.9 | 47.4 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.012 | 0.006 |
| Bond angles (°) | 1.82 | 0.80 |
One crystal used for data collection of each structure.
aValues in parentheses are for the highest-resolution shell.