5AWM
The Crystal Structure of JNK from Drosophila melanogaster Reveals an Evolutionarily Conserved Topology with that of Mammalian JNK Proteins.
Replaces: 4M3AExperimental 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 | CCD |
Collection date | 2012-01-28 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.486, 55.329, 126.717 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.280 - 1.790 |
R-factor | 0.17936 |
Rwork | 0.175 |
R-free | 0.21956 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2xs0 |
RMSD bond length | 0.021 |
RMSD bond angle | 1.982 |
Data reduction software | XDS |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.280 | 1.660 |
High resolution limit [Å] | 1.580 | 1.580 |
Rmerge | 0.062 | 0.794 |
Number of reflections | 51133 | |
<I/σ(I)> | 0.118 | 1.8 |
Completeness [%] | 99.4 | 97.6 |
Redundancy | 4.3 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 295 | 25% (w/v) PEG 4000, 0.1 M Tris-HCl pH 8.5 and 0.2 M MgCl2 |