4UF6
UCH-L5 in complex with ubiquitin-propargyl bound to an activating fragment of INO80G
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-04-07 |
Detector | DECTRIS PILATUS 2M-F |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 152.084, 137.788, 98.916 |
Unit cell angles | 90.00, 102.54, 90.00 |
Refinement procedure
Resolution | 100.990 - 3.690 |
R-factor | 0.23956 |
Rwork | 0.238 |
R-free | 0.26907 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | STRUCTURE OF THE UCH-L5-UBIQUITIN FROM THE |
RMSD bond length | 0.008 |
RMSD bond angle | 1.148 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.740 | 3.980 |
High resolution limit [Å] | 3.690 | 3.690 |
Rmerge | 0.200 | 0.660 |
Number of reflections | 21090 | |
<I/σ(I)> | 5.8 | 1.8 |
Completeness [%] | 97.0 | 90.3 |
Redundancy | 4.2 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 277 | 100 MM MIB PH 5.0, 250 MM AMMONIUM ACETATE, 25% PEG 3350. 4 DEGREES CELSIUS |