Table 1.
Data collection and refinement statistics
| Molecule | D138L mutant | WT |
|---|---|---|
| Space group | P43212 | P3212 |
| Unit cell dimensions | ||
| a, Å | 68.0 | 125.3 |
| b, Å | 68.0 | 125.3 |
| c, Å | 230.1 | 224.7 |
| Resolution, Å | 50–2.3 (2.4–2.3) | 50–3.6 (3.7–3.6) |
| Rmerge, % | 9.0 (71.3) | 8.6 (100) |
| I/σ | 31.2 (2.1) | 23.5 (1.1) |
| Completeness, % | 98.9 (90.9) | 99.9 (100) |
| Redundancy | 13 (9) | 11.3 (10.8) |
| Rcryst,% | 23.9 | 29.5 |
| Rfree,% | 27.4 | 31.8 |
| rmsd bond length, Å | 0.007 | 0.004 |
| rmsd bond angle, ° | 1.106 | 0.893 |
| Protein statistics from Ramachandran plot | ||
| Residues in favored regions | 382 (95.3%) | 958 (82.1%) |
| Residues in allowed regions | 13 (3.2%) | 154 (13.2%) |
| Outliers | 6 (1.5%) | 55 (4.7%) |
The values in parentheses are for the highest-resolution shell. Rmerge is Σ|Ij−〈I〉|/ΣI, where Ij is the intensity of an individual reflection, and 〈I〉 is the mean intensity for multiple recorded reflections. Rcryst is Σ |Fo − Fc|/ ΣFo, where Fo is an observed amplitude and Fc a calculated amplitude; Rfree is the same statistic calculated over a subset, 5%, of the data that have not been used for refinement.