5CWZ
Crystal structure of the kinase domain of human TRAF2 and NCK-interacting protein kinase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-04-21 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 50.215, 123.896, 158.450 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.586 - 2.900 |
| R-factor | 0.2123 |
| Rwork | 0.209 |
| R-free | 0.28140 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2x7f |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.791 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.590 | 3.080 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.692 | |
| Number of reflections | 22760 | |
| <I/σ(I)> | 18.2 | 3.4 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.3 | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 293 | 0.2M Ammonium sulfate, 0.1M Bis-tris (6.2), 35% PEG3350, 9% Ethylene glycol |
