4FMU
Crystal structure of Methyltransferase domain of human SET domain-containing protein 2 Compound: Pr-SNF
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-11-11 |
| Detector | MAR 300 CCD |
| Wavelength(s) | 1.03321 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.547, 77.277, 78.864 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.120 - 2.100 |
| R-factor | 0.1954 |
| Rwork | 0.194 |
| R-free | 0.23500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3H6L |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.000 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.059 | 0.221 |
| Number of reflections | 18501 | |
| <I/σ(I)> | 42.7 | 6.08 |
| Completeness [%] | 97.0 | 82.3 |
| Redundancy | 7 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 20% PEG4000, 10% isoprpanol, 0.1M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
