4CI1
Structure of the DDB1-CRBN E3 ubiquitin ligase bound to thalidomide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-08-22 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 172.180, 172.180, 140.090 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.820 - 2.980 |
| R-factor | 0.1987 |
| Rwork | 0.197 |
| R-free | 0.23320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | DDB1 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.110 |
| 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 | 3.060 |
| High resolution limit [Å] | 2.980 | 2.980 |
| Rmerge | 0.120 | 1.370 |
| Number of reflections | 49202 | |
| <I/σ(I)> | 15.77 | 1.22 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 7.9 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | PROTEIN WAS CRYSTALLIZED FROM 100 MM NA-CACODYLATE; 80 MM NAH2PO4; 120 MM K2HPO4; 800 MM TRI-NA CITRATE., pH 6 |
