4LG4
Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-10-25 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 227.179, 69.771, 148.082 |
Unit cell angles | 90.00, 108.61, 90.00 |
Refinement procedure
Resolution | 29.830 - 2.420 |
R-factor | 0.194 |
Rwork | 0.193 |
R-free | 0.23100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3com |
RMSD bond length | 0.002 |
RMSD bond angle | 0.645 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 140.342 | 2.460 |
High resolution limit [Å] | 2.415 | 2.420 |
Rmerge | 0.052 | 0.537 |
Number of reflections | 83850 | |
<I/σ(I)> | 27.4 | 1.7 |
Completeness [%] | 99.5 | 91.2 |
Redundancy | 4.5 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.7 | 277 | 0.2 M sodium citrate, 15% (w/v) PEG 3350, 0.1 M HEPES, pH 7.7, vapor diffusion, hanging drop, temperature 277K |