4DT6
Co-crystal structure of eIF4E with inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 90 |
Detector technology | CCD |
Collection date | 2007-02-21 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.224, 61.073, 122.439 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.491 - 2.600 |
R-factor | 0.19446 |
Rwork | 0.191 |
R-free | 0.26715 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.017 |
RMSD bond angle | 1.686 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 61.200 | 2.740 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.118 | 0.439 |
Number of reflections | 8533 | |
<I/σ(I)> | 9.1 | 1.7 |
Completeness [%] | 93.0 | 89.3 |
Redundancy | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | The purified protein which contained 100 uM m7-GTP was concentrated to about 7 mg/mL in 20 mM Hepes, pH 7.6, 100 mM KCl, 1mM DTT, and 0.1 mM EDTA for crystallization. The m7-GTP-bound eIF4e protein was crystallized with 1:1 ratio of protein solution to reservoir solution of 17-20% PEG-3350 and 0.1-0.4M Na formate, VAPOR DIFFUSION, SITTING DROP, temperature 293K |