2V74
Crystal structure of coactivator-associated arginine methyltransferase 1 (CARM1), in complex with S-adenosyl-homocysteine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-09-18 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 74.879, 98.691, 207.224 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.700 |
R-factor | 0.226 |
Rwork | 0.223 |
R-free | 0.27300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ori |
RMSD bond length | 0.009 |
RMSD bond angle | 1.247 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.850 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.090 | 0.380 |
Number of reflections | 40542 | |
<I/σ(I)> | 16.8 | 3 |
Completeness [%] | 99.2 | 99.2 |
Redundancy | 6.6 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 1.6M DI-AMMONIUM HYDROGENPHOSPHATE, 100MM HEPES PH 7.5. |