4X41
Crystal Structure of Protein Arginine Methyltransferase PRMT8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-05-22 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 2 2 21 |
| Unit cell lengths | 68.159, 78.236, 203.861 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.727 - 3.500 |
| R-factor | 0.2339 |
| Rwork | 0.231 |
| R-free | 0.28200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.019 |
| Data reduction software | SCALA |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_1819) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 20.000 | 3.620 |
| High resolution limit [Å] | 3.500 | 7.420 | 3.500 |
| Rmerge | 0.196 | 0.064 | 0.478 |
| Rmeas | 0.239 | 0.078 | 0.586 |
| Rpim | 0.133 | 0.043 | 0.332 |
| Total number of observations | 38801 | ||
| Number of reflections | 13561 | ||
| <I/σ(I)> | 5.7 | ||
| Completeness [%] | 94.7 | 88.8 | 97.1 |
| Redundancy | 2.9 | 2.7 | 2.8 |
| CC(1/2) | 0.993 | 0.692 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 150mM D-glucose, 100mM HEPES/MOPS pH7.5, 40% Glycerol/PEG4000 |






