4CI2
Structure of the DDB1-CRBN E3 ubiquitin ligase bound to lenalidomide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-09-03 |
| Detector | DECTRIS PILATUS 2M |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 172.110, 172.110, 139.840 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.710 - 2.950 |
| R-factor | 0.1951 |
| Rwork | 0.193 |
| R-free | 0.23390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | DDB1 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.180 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.11.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.030 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmerge | 0.130 | 1.500 |
| Number of reflections | 50544 | |
| <I/σ(I)> | 14.33 | 1.01 |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 7.04 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | PROTEIN WAS CRYSTALLIZED FROM 100 MM NA-CACODYLATE PH 6.2, 80 MM NAH2PO4, 120 MM K2HPO4, 950 MM TRI-NA CITRATE. |
