5YJ1
Mouse Cereblon thalidomide binding domain complexed with R-form thalidomide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-15 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.9 |
| Spacegroup name | H 3 |
| Unit cell lengths | 201.615, 201.615, 123.572 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.780 - 2.000 |
| R-factor | 0.20025 |
| Rwork | 0.199 |
| R-free | 0.22766 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wx2 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.258 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.050 |
| High resolution limit [Å] | 2.000 | 1.980 |
| Rmerge | 0.078 | 0.493 |
| Number of reflections | 130317 | 12954 |
| <I/σ(I)> | 20.6 | 3.9 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 5.8 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 1.0M ammonium sulfate 0.1M sodium acetate (pH5.0) |
