5LGQ
Crystal structure of mouse CARM1 in complex with ligand P2C3s
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-02-24 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.073 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 74.706, 99.011, 207.306 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.152 - 2.110 |
R-factor | 0.189 |
Rwork | 0.187 |
R-free | 0.23600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5ih3 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.530 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((dev_2386: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.152 | 2.150 |
High resolution limit [Å] | 2.110 | 2.110 |
Rmerge | 0.150 | 2.021 |
Number of reflections | 89266 | |
<I/σ(I)> | 9 | 0.7 |
Completeness [%] | 99.9 | 99.6 |
Redundancy | 6.5 | 4.7 |
CC(1/2) | 0.998 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 100 mM Tris-HCl pH 8.5 14% PEG 3350 200 mM A.S. |