7QPB
Catalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid foldamer-peptide macrocycle
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 | PIXEL |
| Collection date | 2021-05-06 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9724 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 149.910, 59.050, 67.300 |
| Unit cell angles | 90.00, 95.47, 90.00 |
Refinement procedure
| Resolution | 29.530 - 2.342 |
| R-factor | 0.2173 |
| Rwork | 0.215 |
| R-free | 0.26260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c4z |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.620 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.17.1_3660: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.530 | 2.426 |
| High resolution limit [Å] | 2.342 | 2.342 |
| Rmerge | 0.066 | 0.611 |
| Rmeas | 0.078 | 0.725 |
| Rpim | 0.042 | 0.387 |
| Number of reflections | 24491 | 2402 |
| <I/σ(I)> | 11.91 | 1.91 |
| Completeness [%] | 98.3 | 97.05 |
| Redundancy | 3.5 | 3.4 |
| CC(1/2) | 0.998 | 0.669 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 277 | 12% PEG 8000, 0.1 M sodium cacodylate, 0.1 M calcium acetate pH 5.5 |
