9Q74
Crystal structure of T. brucei EIF4E5 in complex with EIF4G1 peptide and cap-4.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 2 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-12-09 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.98011 |
| Spacegroup name | P 3 2 1 |
| Unit cell lengths | 140.380, 140.380, 41.350 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 22.330 - 1.570 |
| R-factor | 0.14444 |
| Rwork | 0.142 |
| R-free | 0.18258 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.810 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0430) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 121.570 | 1.800 |
| High resolution limit [Å] | 1.570 | 1.570 |
| Number of reflections | 39727 | 1986 |
| <I/σ(I)> | 11.3 | |
| Completeness [%] | 94.4 | |
| Redundancy | 7.1 | |
| CC(1/2) | 0.999 | 0.654 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | Complex at 9.4 mg/mL in 20 mM Tris-HCl, 150 mM NaCl, 2 mM DTT, pH 8.0 (pre-incubated with cap-4) with crystallization buffer containing 0.12 M monosaccharides (D-glucose, D-mannose, D-galactose, L-fucose, D-xylose, N-acetyl-D-Glucosamine), 0.1 M buffer system 1 pH 6.5 (imidazole, MES), 30% precipitant Mix2 (ethylene glycol, PEG 8000) from Morpheus Screen |






