Table 2. Data collection and refinement statistics of EcoDMT mutants.
| EcoDMT E129Q | EcoDMT E129A | EcoDMT H236A | |
|---|---|---|---|
| Data collection | |||
| Space group | C2 | C2 | C2 |
| Cell dimensions | |||
| a, b, c (Å) | 151.3, 81.8, 96.5 | 149.1, 80.8, 96.4 | 150.4, 81.8, 96.4 |
| α, β, γ (°) | 90.0, 107.6, 90.0 | 90.0, 107.4, 90.0 | 90.0, 107.5, 90.0 |
| Resolution (Å) | 50–3.6 (3.7–3.6)* | 50–3.9 (4.0–3.9) | 50–3.7 (3.8–3.7) |
| Rmerge (%) | 6.3 (154) | 5.9 (112.6) | 5.6 (140.9) |
| CC½ (%) | 99.8 (81.7) | 99.7 (79.0) | 99.9 (87.0) |
| I/σI | 12.8 (1.8) | 13.4 (1.8) | 17.2 (2.0) |
| Completeness (%) | 98.7 (99.8) | 98.4 (98.3) | 98.9 (99.9) |
| Redundancy | 6.7 (7.0) | 6.8 (6.6) | 11.2 (11.4) |
| Refinement | |||
| Resolution (Å) | 12–3.6 | 12–3.9 | 12–3.7 |
| No. reflections | 12658 | 9644 | 11546 |
| Rwork/Rfree (%) | 22.1/26.5 | 21.1/26.2 | 23.2/26.8 |
| No. atoms | |||
| Protein | 3,780 | 3,776 | 3,775 |
| Ligand/ion | — | — | — |
| B factors | |||
| Protein | 213.4 | 211.2 | 201.3 |
| Ligand/ion | — | — | — |
| r.m.s. deviations | |||
| Bond lengths (Å) | 0.002 | 0.002 | 0.002 |
| Bond angles (°) | 0.49 | 0.49 | 0.50 |
*Values in parentheses are for highest-resolution shell.