3Q87
Structure of E. cuniculi Mtq2-Trm112 complex responible for the methylation of eRF1 translation termination factor
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 | CCD |
Collection date | 2008-04-20 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.214 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 42.115, 74.316, 96.754 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.377 - 1.997 |
R-factor | 0.2051 |
Rwork | 0.202 |
R-free | 0.25580 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.106 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SHARP |
Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.220 |
High resolution limit [Å] | 1.997 | 2.000 |
Number of reflections | 33750 | |
<I/σ(I)> | 8.3 | 2 |
Completeness [%] | 97.9 | 96.9 |
Redundancy | 2.4 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 310 | 20% PEG4000, 10% isopropanol, 100mM Hepes, pH 7.5, VAPOR DIFFUSION, temperature 310K |