6OMU
Structure of human Bruton's Tyrosine Kinase in complex with Evobrutinib
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-20 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 72.173, 104.520, 37.983 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.000 - 1.410 |
| R-factor | 0.192 |
| Rwork | 0.190 |
| R-free | 0.22600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5p9g |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.391 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.460 |
| High resolution limit [Å] | 1.410 | 1.410 |
| Rmerge | 0.118 | 0.566 |
| Number of reflections | 55920 | 5512 |
| <I/σ(I)> | 15 | 3.5 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 5.4 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 20% PEG 3350, 0.1 M Bis Tris Propane pH 7.5, 0.2 M Sodium acetate trihydrate |
