7F2X
Crystal structure of MEK1 C121S mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL32XU |
Synchrotron site | SPring-8 |
Beamline | BL32XU |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-11-24 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 1.0 |
Spacegroup name | F 2 2 2 |
Unit cell lengths | 49.498, 156.504, 179.156 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.789 - 2.007 |
R-factor | 0.2159 |
Rwork | 0.215 |
R-free | 0.23240 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3eqc |
RMSD bond length | 0.002 |
RMSD bond angle | 0.583 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | BALBES |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.789 | 2.130 |
High resolution limit [Å] | 2.007 | 2.007 |
Rmerge | 0.198 | 1.207 |
Number of reflections | 23080 | 3547 |
<I/σ(I)> | 5.59 | 1.15 |
Completeness [%] | 97.8 | 95 |
Redundancy | 6.8 | 6.6 |
CC(1/2) | 0.973 | 0.690 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | PEG 3350 26%, 100 mM Bicine, 150 mM NH4F, 1% glycerol |