Table 1. Crystallographic data and refinement.
| Holo native | Apo native | Apo Se methionine | |||
|---|---|---|---|---|---|
| Diffraction data | |||||
| Wavelength | Native: 0.9794 Å | Native: 0.97937 Å | Se peak: 0.97955 Å | Se inflection: 0.979700 Å | Se remote: 0.97565 Å |
| Unit cell (Å) | P41212 | P41212 | P41212 | P41212 | P41212 |
| a,b = 143.81 | a,b = 142.49 | a,b = 144.60 | a,b = 144.64 | a,b = 144.60 | |
| c = 254.57 | c = 251.81 | c = 256.93 | c = 256.08 | c = 256.73 | |
| β,γ = 90° | β,γ = 90° | β,γ = 90° | β,γ = 90° | β,γ = 90° | |
| Resolution (Å) | 30.0-3.2 | 40-2.4 | 40-3.0 | 40-3.0 | 40-3.0 |
| ()=Highest resolution shell | (3.28-3.20) | (2.66-2.60) | (3.11-3.00) | (3.11-3.00) | (3.11-3.00) |
| -Rmerge (%) | 30.9 (68.0) | 13.5 (87.3) | 10.0 (24.1) | 9.0 (17.6) | 9.4 (18.1) |
| <l>/<s(l)> | 5.1 (2.5) | 17.2 (3.0) | 16.2 (7.5) | 15.5 (8.2) | 15.5 (8.0) |
| Completeness (%) | 89 (91) | 100 (100) | 100 (100) | 100 (100) | 100 (100) |
| Redundancy | 4.2 (4.3) | 8.7 (8.6) | 7.3 (7.5) | 6.1 (6.1) | 6.6 (6.5) |
| Wilson B Factor (Å2) | 52.3 | 54.9 | |||
| Phasinga | |||||
| Figure of merit | 0.37 | ||||
| Refinement | |||||
| Reflections | 26910 | 76341 | |||
| Atoms: | |||||
| Total | 12,543 | 13,373 | |||
| Protein (non-H) | 12,242 | 12,594 | |||
| Solvent | 1 | 748 | |||
| AMP | 46 | 46 | |||
| ThDP | 52 | 0 | |||
| Oxaloacetate | 18 | 0 | |||
| Mg | 2 | 0 | |||
| Rwork (%) | 23.7 (30.0) | 18.30 (30.6) | |||
| Rfree ^(%) | 30.3 (34.6) | 24.8 (39.8) | |||
| RMSD bonds (Å) | 0.026 | 0.014 | |||
| RMSD angles (°) | 2.40 | 1.18 | |||
| Ramachandran statistics (%) | |||||
| Generously allowed | 0.7 | 0.1 | |||
| Additional allowed | 15.7 | 10.1 | |||
| Most favourable | 83.6 | 89.8 | |||
| Disallowed | 0.1 | None | |||
a
Anomalous substructure was solved from the MAD data, and figure of merit was estimated by PHASER for SAD data. SAD data were used to calculate phases.
^
5% of reflections were used for Rfree set.