5MI3
Structure of phosphorylated translation elongation factor EF-Tu from E. coli
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 | 2015-11-02 |
Detector | DECTRIS PILATUS3 R CdTe 300K |
Wavelength(s) | 1.000 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 68.200, 244.400, 61.740 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.771 - 2.800 |
R-factor | 0.1556 |
Rwork | 0.153 |
R-free | 0.19840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1efc |
RMSD bond length | 0.008 |
RMSD bond angle | 1.027 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10_2152: ???)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 45.800 |
High resolution limit [Å] | 2.800 |
Rmerge | 0.134 |
Number of reflections | 25588 |
<I/σ(I)> | 19.4 |
Completeness [%] | 97.1 |
Redundancy | 7.2 |
CC(1/2) | 1.000 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.2 M NaCl, 0.1 M MES and 10 % PEG4000. |