6MOM
Crystal structure of human Interleukin-1 receptor associated Kinase 4 (IRAK 4, CID 100300) in complex with compound NCC00371481 (BSI 107591)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-12-21 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 138.290, 141.910, 87.890 |
Unit cell angles | 90.00, 126.22, 90.00 |
Refinement procedure
Resolution | 45.729 - 2.100 |
R-factor | 0.1682 |
Rwork | 0.167 |
R-free | 0.20660 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2NRU as per Morda |
RMSD bond length | 0.007 |
RMSD bond angle | 0.921 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MoRDa |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 45.729 | 45.729 | 2.150 |
High resolution limit [Å] | 2.100 | 9.390 | 2.100 |
Rmerge | 0.090 | 0.028 | 0.433 |
Rmeas | 0.097 | 0.030 | 0.470 |
Number of reflections | 79032 | 916 | 5694 |
<I/σ(I)> | 15.89 | 43.83 | 5.1 |
Completeness [%] | 98.9 | 96.6 | 96.2 |
Redundancy | 7.47 | 7.309 | 6.568 |
CC(1/2) | 0.999 | 0.999 | 0.923 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 9.5 mg/ml IRAK4 (CID100300, Batch BOS047020B) in 20 mM Tris-HCl, pH 8.0, 1 mM DTT, with 1 mM BSI107659 (NCGC00371481) in DMSO, crystallization condition: Microlytic screen MCSG1, E10: 0.2 M ammonium tartrate dibasic, 20% PEG3350, cryoprotectant: 20% ethylene glycol with 1 mM compound, tray 286446 e10, puck: xvc2-1 |