7OW2
E3 RING ligase binding domain with peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-18 |
| Detector | OXFORD TITAN CCD |
| Wavelength(s) | 0.987 |
| Spacegroup name | P 61 |
| Unit cell lengths | 108.119, 108.119, 137.142 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 93.630 - 2.170 |
| R-factor | 0.2095 |
| Rwork | 0.208 |
| R-free | 0.24750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2iwg |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.397 |
| Data reduction software | ADDREF |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 93.640 | 2.290 |
| High resolution limit [Å] | 2.170 | 2.200 |
| Rmerge | 0.103 | |
| Number of reflections | 47982 | 1398 |
| <I/σ(I)> | 12.6 | |
| Completeness [%] | 99.7 | |
| Redundancy | 6.4 | |
| CC(1/2) | 0.997 | 0.963 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 6.7 | 297 | 23% PEG 6K, 0.1 M NaCl, 50mM HEPES pH 6.7 |
