5L3B
Human LSD1/CoREST: LSD1 D556G mutation
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 | 2014-12-06 |
Detector | DECTRIS PILATUS 300K |
Wavelength(s) | 0.97626 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 119.088, 179.122, 234.411 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 3.300 |
R-factor | 0.19483 |
Rwork | 0.195 |
R-free | 0.20783 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 2v1d |
RMSD bond length | 0.008 |
RMSD bond angle | 1.308 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | REFMAC |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.450 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.131 | 0.613 |
Number of reflections | 37869 | |
<I/σ(I)> | 7.2 | 1.7 |
Completeness [%] | 99.6 | 99.6 |
Redundancy | 3.8 | 3.9 |
CC(1/2) | 0.988 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | Tartrate 1-1.4 M, ADA 100 mM pH 6.5 |