5ME5
Crystal Structure of eiF4E from C. melo bound to a eIF4G peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALBA BEAMLINE XALOC |
| Synchrotron site | ALBA |
| Beamline | XALOC |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-12-16 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.094, 70.352, 42.798 |
| Unit cell angles | 90.00, 93.62, 90.00 |
Refinement procedure
| Resolution | 29.332 - 1.900 |
| R-factor | 0.1877 |
| Rwork | 0.186 |
| R-free | 0.21350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.757 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.21) |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11_2567: ???)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 42.713 | 29.332 | 2.000 |
| High resolution limit [Å] | 1.900 | 6.010 | 1.900 |
| Rmerge | 0.031 | 0.608 | |
| Number of reflections | 17809 | ||
| <I/σ(I)> | 11.2 | 19.8 | 1.3 |
| Completeness [%] | 99.8 | 99.2 | 99.7 |
| Redundancy | 3.7 | 3.7 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 4.5 | 293 | ammonium sulphate, sodium acetate |
