TABLE 1.
Data collection, phasing, and refinement statistics for x-ray crystallography of the FYCO1 LIR peptide-LC3B complex
| Data collection | |
| Wave length (Å) | 0.9 |
| Unit cell a, b, c (Å) | 40.7, 39.1, 42.8 |
| Unit cell α, β, γ (°) | 90.00, 115.1, 90.00 |
| Space group | P21 |
| Resolution range (Å) | 50.0–1.53 (1.56–1.53) |
| No. of unique reflections | 17,994 |
| Completeness (%) | 96.4 (97.9) |
| Rmerge (%) | 5.2 (9.8) |
| 〈I/σ(I)〉 | 49.7 (27.5) |
| Redundancy | 3.6 (3.7) |
| Wilson B-factor (Å2) | 12.0 |
| Refinement statistics | |
| Resolution range (Å) | 19.58–1.53 |
| No. of reflections used | 17,088 |
| Free R reflections (%) | 5 |
| R/Rfree | 0.175/0.217 |
| RMSDa bond length (Å) | 0.023 |
| RMSDa bond angle (°) | 2.010 |
| Average atomic B-factor of protein (Å2) | 11.7 |
| Average atomic B-factor of ligand (Å2) | 20.4 |
| Average atomic B-factor of solvent atoms (Å2) | 20.6 |
| Ramachandran analysis (%) | |
| Residues in most favored regions | 94.1 |
| Residues in additional allowed regions | 5.9 |
| Residues in generously allowed regions | 0.0 |
| Residues in disallowed regions | 0.0 |
a RMSD, root mean square deviation.