Table 1.
Data collection, phasing, and refinement statistics
| Native TraM58–127 | SeMet-TraM58–127 | Native TraM58–127-E88L | ||
|---|---|---|---|---|
| Data collection | ||||
| Space group | I4 | I4 | I4 | |
| Cell dimensions | ||||
| a, b, c (Å) | 51.73, 51.73, 49.59 | 51.68, 51.68, 49.73 | 50.94, 50.94, 46.55 | |
| α, β, γ (deg) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | |
| Inflection | Remote | |||
| Wavelength | 1.116975 | 0.979617 | 1.019440 | 1.115869 |
| Resolution (Å) | 1.40 | 1.42 | 1.34 | 1.80 |
| Rsym or Rmerge | 0.035 (0.373) | 0.051 (0.448) | 0.055 (0.567) | 0.047 (0.362) |
| I/σI | 27.6 (1.8) | 23.8 (3.4) | 23.7 (2.4) | 25.1 (2.4) |
| Completeness (%) | 99.1 (86.6) | 98.1 (96.6) | 97.8 (96.1) | 98.6 (84.1) |
| Redundancy | 3.6 (2.8) | 4.1 (3.9) | 4.1 (3.9) | 3.6 (2.2) |
| Refinement | ||||
| Resolution (Å) | 36.6–1.40 | 36.0–1.80 | ||
| No. of reflections | 12 201 | 5288 | ||
| Rwork/Rfree | 0.193/0.224 | 0.182/0.244 | ||
| No. of atoms | ||||
| Protein | 551 | 543 | ||
| Ligand/ion | 0 | 0 | ||
| Water | 55 | 42 | ||
| B-factors | ||||
| Protein | 16.6 | 23.6 | ||
| Ligand/ion | ||||
| Water | 24.6 | 27.2 | ||
| RMS deviations | ||||
| Bond lengths (Å) | 0.010 | 0.012 | ||
| Bond angles (deg) | 1.233 | 1.193 | ||
| Highest resolution shell for the native TraM58–127 crystal is 1.42–1.40, for the selenomethionine derivative is 1.44–1.42 (inflection) and 1.36–1.34 (remote), and for the native TraM58–127-E88L crystal is 1.83–1.80. | ||||