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 |
