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 |