9Q78
Crystal structure of T. cruzi EIF4E6 in complex with EIF4G5 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-07-19 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.893, 112.694, 100.024 |
| Unit cell angles | 90.00, 97.96, 90.00 |
Refinement procedure
| Resolution | 49.580 - 2.100 |
| R-factor | 0.20454 |
| Rwork | 0.201 |
| R-free | 0.26977 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.840 |
| 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] | 112.690 | 2.190 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Number of reflections | 37674 | 1884 |
| <I/σ(I)> | 7.5 | |
| Completeness [%] | 94.4 | |
| Redundancy | 7 | |
| CC(1/2) | 0.997 | 0.767 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | Complex at 7.3 mg/mL in 20 mM Tris-HCl, 150 mM NaCl, 2 mM DTT, pH 8.0 with crystallization buffer containing 80 mM Monosaccharides (0.2 M D-glucose, 0.2 M D-mannose, 0.2 M D-galactose, 0.2 M L-fucose, 0.2 M D-xylose, 0.2 M N-acetyl-D-glucosamine), 100 mM Buffer System 1 (pH 6.5; 0.4 M imidazole, 0.6 M MES monohydrate), and 37.5% (w/v) Precipitant Mix 4 (25% v/v MPD, 25% v/v PEG 1000, 25% w/v PEG 3350) |






