TABLE 1.
acRAF X-ray data collection and model refinement statistics
Statistics for the highest resolution shell are shown in parentheses.
| Statistics | Value |
|---|---|
| Wavelength (Å) | 0.9791 |
| Resolution range (Å) | 51.1 − 1.30 (1.34–1.30) |
| Space group | P41 |
| Unit cell (Å,°) | a = b = 51.1, c = 60.9; α = β = γ = 90 |
| Total reflections recorded | 253,115 (169,41) |
| Unique reflections | 37,451 (2610) |
| Multiplicity | 6.7 (6.5) |
| Completeness (%) | 96.9 (92.6) |
| Mean I/σ(I) | 17.2 (2.05) |
| Wilson B-factor (Å2) | 23.1 |
| CC(1/2) | 99.9% (69.4%) |
| Model Rwork | 0.203 (0.211) |
| Model Rfree | 0.204 (0.241) |
| Number of chains | 2 |
| Number of modeled residues (chain A/chain B) | 83/78 |
| Number of non-hydrogen atoms | 1452 |
| Macromolecules | 1305 |
| Formate | 18 |
| Water | 127 |
| Ni2+a | 2 |
| Protein residues | 336 |
| Geometric deviations (rms) | |
| bonds (Å) | 0.001 |
| angles (°) | 1.03 |
| Ramachandran statistics (%) | |
| Favored | 97.8 |
| Additionally allowed | 2.2 |
| Generously allowed | 0 |
| Disallowed | 0 |
| Average B-factor (Å2) | |
| Protein main chain | 29.5 |
| Protein side chains | 33.6 |
| Solvent (water) | 39.1 |
a The divalent metal ion was defined as Ni2+ during the refinement process based on its location between histidine tags, combined with the plausibility of contamination from nickel-bound chromatography columns.