Table 1.
Crystallographic data and refinement statistics for free TRIAP1 and the TRIAP1-SLMO1 complex
| Crystal parameters | TRIAP1 | TRIAP1-SLMO1 complex | |
|---|---|---|---|
| Space group | P21 | P1 | |
| Cell dimensions (Å) | a = 75.4, b = 56.0, c = 100.3 | a = 79.6, b = 80.9, c = 98.0 | |
| β = 106.4 | α = 87.3, β = 85.6, γ = 89.9 | ||
| Molecules per asymmetric unit | 2 | 8 | |
| Data collection | |||
| Beamline | DLS I03 | DLS I03 | |
| Wavelength (Å) | 0.98 | 0.98 | |
| Resolution (Å) | 2.12–48.41 (2.12–2.18) | 3.58–97.62 (3.58–3.67) | |
| Unique observations | 45,307 (3,176) | 28,326 (2,108) | |
| Rmerge | 0.093 (0.585) | 0.108 (0.544) | |
| <I>/σI | 9.3 (2.2) | 11.6 (2.7) | |
| Completeness (%) | 98.7 (94.0) | 98.9 (98.7) | |
| Redundancy | 3.6 (3.2) | 3.5 (3.5) | |
| Average B value (Å2) | 35.5 | 85.6 | |
| Refinement | |||
| Rwork/Rfree (%) | 19.8/24.2 | 27.5/30.9 | |
| Protein residues in asymmetric unit | 841 | 2,218 | |
| Number of ligands | 2 maltose | 4 maltose | |
| Number of waters | 266 | 0 | |
| Rmsd stereochemistry | |||
| Bond length (Å) | 0.013 | 0.011 | |
| Bond angles (º) | 1.47 | 1.66 | |
| Ramachandran analysis | |||
| Residues in favoured regions | 98.8% | 96.3% | |
| Residues in allowed regions | 100% | 100% | |