3O71
Crystal structure of ERK2/DCC peptide complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-10 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9794 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 87.178, 87.178, 94.459 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.230 - 1.950 |
R-factor | 0.20097 |
Rwork | 0.199 |
R-free | 0.24000 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 0.976 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.980 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.670 | |
Number of reflections | 30642 | |
<I/σ(I)> | 3.59 | |
Completeness [%] | 99.9 | 100 |
Redundancy | 10.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.9 | 293 | 0.1 M HEPES, pH 6.9, 18% PEG3350, and 0.12 M KSCN, VAPOR DIFFUSION, HANGING DROP, temperature 293K |