7M4M
Crystal structure of RBR E3 ligase RNF216 with ubiquitin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-07-08 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.953724 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 81.871, 81.871, 248.656 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.460 - 2.390 |
R-factor | 0.2049 |
Rwork | 0.200 |
R-free | 0.24680 |
Structure solution method | SAD |
Starting model (for MR) | RNF216/ubiquitin |
RMSD bond length | 0.002 |
RMSD bond angle | 0.482 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | AutoSol |
Refinement software | PHENIX (dev_3965) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.510 | 2.732 |
High resolution limit [Å] | 2.387 | 2.387 |
Rmerge | 0.126 | 2.276 |
Rmeas | 0.132 | 2.378 |
Rpim | 0.037 | 0.678 |
Number of reflections | 18242 | 913 |
<I/σ(I)> | 13.8 | 1.4 |
Completeness [%] | 52.6 | 8.1 |
Redundancy | 13 | 12.1 |
CC(1/2) | 0.998 | 0.470 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 15% PEG 6000, 0.18 M NaCl, 0.09 M Na HEPES pH7.0, 0.1 M KCl |