3K54
Structures of human Bruton's tyrosine kinase in active and inactive conformations suggests a mechanism of activation for TEC family kinases.
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 | 2009-06-05 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 73.438, 104.622, 38.107 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.400 - 1.940 |
| R-factor | 0.20184 |
| Rwork | 0.199 |
| R-free | 0.25813 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k2p |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.045 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.010 |
| High resolution limit [Å] | 1.940 | 1.940 |
| Rmerge | 0.083 | 0.619 |
| Number of reflections | 21816 | |
| <I/σ(I)> | 32 | 3.31 |
| Completeness [%] | 99.2 | 99.2 |
| Redundancy | 6.8 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 273 | 20% Peg5000 MME, 0.2M Ammonium Acetate, 0.1M Bis-Tris pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 273K |
