2W97
Crystal Structure of eIF4E Bound to Glycerol and eIF4G1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-25 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 84.106, 38.201, 93.687 |
| Unit cell angles | 90.00, 101.51, 90.00 |
Refinement procedure
| Resolution | 28.020 - 2.290 |
| R-factor | 0.199 |
| Rwork | 0.197 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2v8w |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.292 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.080 | 0.360 |
| Number of reflections | 26638 | |
| <I/σ(I)> | 5.7 | 4.3 |
| Completeness [%] | 99.6 | 99.7 |
| Redundancy | 4.4 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 60% AMMONIUM SULPHATE, 100MM TRIS-HCL PH 8.0, 1% PEG400 |
