6NZM
Brutons tyrosine kinase in complex with compound 50.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-08-14 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.297, 71.709, 104.410 |
| Unit cell angles | 90.00, 89.95, 90.00 |
Refinement procedure
| Resolution | 31.310 - 1.720 |
| R-factor | 0.179 |
| Rwork | 0.175 |
| R-free | 0.24830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.944 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.760 |
| High resolution limit [Å] | 1.730 | 4.690 | 1.730 |
| Rmerge | 0.107 | 0.052 | 0.915 |
| Rmeas | 0.127 | 0.062 | 1.076 |
| Rpim | 0.067 | 0.033 | 0.560 |
| Total number of observations | 213239 | ||
| Number of reflections | 59589 | 2916 | 3005 |
| <I/σ(I)> | 5.1 | ||
| Completeness [%] | 99.4 | 94.2 | 100 |
| Redundancy | 3.6 | 3.4 | 3.6 |
| CC(1/2) | 0.993 | 0.617 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 298 | 0.2M Ammonium Tartrate, 20% PEG3350 |
