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 |