5D7A
Crystal structure of the kinase domain of TRAF2 and NCK-interacting protein kinase with NCB-0846
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 | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 212.620, 124.972, 49.897 |
| Unit cell angles | 90.00, 96.32, 90.00 |
Refinement procedure
| Resolution | 46.920 - 2.900 |
| R-factor | 0.1868 |
| Rwork | 0.184 |
| R-free | 0.23910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2x7f |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.822 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.920 | 3.080 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.117 | |
| Number of reflections | 28803 | |
| <I/σ(I)> | 15.8 | 2.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.7 | 7.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 293 | 0.2M Ammonium sulfate 0.1M Bis-tris (5.6) 15% PEG3350 7% Ethyleneglycol |
