2EVA
Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX14.1 |
Synchrotron site | SRS |
Beamline | PX14.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-01-01 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.488 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 58.400, 144.300, 134.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.219 |
Rwork | 0.212 |
R-free | 0.23100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.500 |
Data reduction software | PROCOR |
Data scaling software | PROCOR |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 35174 | |
Completeness [%] | 91.3 | 70.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 0.7M NaCitrate, 0.1M Tris-HCL, 0.2M NaCl, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |