2CLQ
Structure of mitogen-activated protein kinase kinase kinase 5
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-10-23 |
Detector | MARRESEARCH |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 78.606, 78.606, 423.279 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.300 |
R-factor | 0.204 |
Rwork | 0.201 |
R-free | 0.25700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HOMOLOGY MODEL |
RMSD bond length | 0.014 |
RMSD bond angle | 1.526 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.000 | 2.390 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.100 | 0.590 |
Number of reflections | 35817 | |
<I/σ(I)> | 17.7 | 1.9 |
Completeness [%] | 99.3 | 93.9 |
Redundancy | 14.9 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 25% PEG3350 0.17M, (NH4)2SO4 15% GLYCEROL |