6RFP
ERK2 MAP kinase with mutations at Helix-G
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-02-05 |
Detector | DECTRIS PILATUS 300K |
Wavelength(s) | 0.972 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 48.740, 68.810, 60.810 |
Unit cell angles | 90.00, 110.14, 90.00 |
Refinement procedure
Resolution | 45.800 - 1.740 |
R-factor | 0.14652 |
Rwork | 0.144 |
R-free | 0.19726 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4s31 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.967 |
Data reduction software | MOSFLM |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.800 | 1.790 |
High resolution limit [Å] | 1.740 | 1.740 |
Number of reflections | 38438 | 2840 |
<I/σ(I)> | 16.1 | |
Completeness [%] | 99.4 | |
Redundancy | 3.7 | |
CC(1/2) | 0.990 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 1.8 M ammonium sulfate 0.1 M Bis-tris pH 6.8 or 6.5 2% (w/v) PEG 550 |