6LF3
3D domain-swapped dimer of the maltose-binding protein fused to a fragment of the protein-tyrosine kinase 2-beta
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 2 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-03-21 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.980 |
| Spacegroup name | P 1 |
| Unit cell lengths | 78.780, 92.740, 93.610 |
| Unit cell angles | 112.46, 101.66, 94.93 |
Refinement procedure
| Resolution | 47.900 - 3.200 |
| R-factor | 0.2459 |
| Rwork | 0.244 |
| R-free | 0.28390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5bmy |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.348 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0257) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.900 | 3.300 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.105 | 0.841 |
| Rmeas | 0.126 | 1.000 |
| Rpim | 0.069 | 0.567 |
| Number of reflections | 37579 | 3539 |
| <I/σ(I)> | 3.1 | 1.03 |
| Completeness [%] | 96.8 | 90.43 |
| Redundancy | 3.8 | |
| CC(1/2) | 0.996 | 0.560 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 10.5 | 298 | 30% (v/v) PEG 400, 0.1M CAPS/Sodium hydroxide |
