6NYH
Structure of human RIPK1 kinase domain in complex with GNE684
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-08-08 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.980, 97.034, 125.238 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.517 - 2.100 |
R-factor | 0.2056 |
Rwork | 0.203 |
R-free | 0.24640 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ith |
RMSD bond length | 0.008 |
RMSD bond angle | 0.935 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.10.1-2155_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.520 | 2.160 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.106 | 0.872 |
Number of reflections | 32257 | |
<I/σ(I)> | 8.8 | 1.6 |
Completeness [%] | 94.4 | 96.6 |
Redundancy | 5.7 | 5.7 |
CC(1/2) | 0.992 | 0.723 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 277 | 0.1 M Bis Tris Propane buffer (pH 6.5), 0.2 M sodium iodide, 20% PEG3350 |