2Y43
Rad18 ubiquitin ligase RING domain structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-17 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 104.646, 29.357, 69.736 |
| Unit cell angles | 90.00, 125.05, 90.00 |
Refinement procedure
| Resolution | 42.860 - 1.800 |
| R-factor | 0.1774 |
| Rwork | 0.175 |
| R-free | 0.22311 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.207 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.5.0099) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.840 | 1.890 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.090 | 0.620 |
| Number of reflections | 16560 | |
| <I/σ(I)> | 24.3 | 2.5 |
| Completeness [%] | 99.9 | 99.2 |
| Redundancy | 17.3 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 15% PEG 3350, 100 MM AMMONIUM ACETATE, 100 MM BIS-TRIS PH 5.5 . |
