Table 4. Structure solution and refinement.
Values in parentheses are for the highest resolution shell.
| Resolution range (Å) | 46.03–1.65 (1.69–1.65) |
| Completeness (%) | 96.96 (73.95) |
| σ Cutoff | None |
| No. of reflections, working set | 42685 (2362) |
| No. of reflections, test set | 4916 (270) |
| Final R cryst † | 0.170 (0.254) |
| Final R free ‡ | 0.214 (0.323) |
| Cruickshank DPI | 0.1067 |
| No. of non-H atoms | |
| Protein§ | 3181 |
| PLP–Tris | 23 |
| Ethylene glycol | 24 |
| Waters§ | 458 |
| Total | 3686 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.011 |
| Angles (°) | 1.675 |
| Average B factors¶ (Å2) | |
| Protein | 15.0 |
| PLP–Tris | 11.8 |
| Ethylene glycol | 38.2 |
| Waters | 27.6 |
| Ramachandran plot | |
| Favored regions (%) | 98 |
| Additionally allowed (%) | 2 |
| Unmodelled/incomplete residues (%) | 1.3 |
†
R
cryst is the conventional crystallographic R factor; R
cryst =
, where F
obs and F
calc are the observed and calculated structure factors, respectively.
‡
R free was calculated as for R cryst but was calculated for 10% of the reflections that were chosen at random and omitted from the refinement process (Brünger, 1992 ▸).
§
The corresponding two atoms with 50% occupancy in the double conformers were counted separately.
¶
The average temperature factor was calculated based on the number of non-H atoms.