4H12
The crystal structure of methyltransferase domain of human SET domain-containing protein 2 in complex with S-adenosyl-L-homocysteine
Replaces: 3H6LExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-03-18 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97935 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 52.293, 76.663, 78.093 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.360 - 2.060 |
| R-factor | 0.20953 |
| Rwork | 0.207 |
| R-free | 0.24904 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2r3a |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.251 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.030 |
| High resolution limit [Å] | 1.991 | 5.430 | 1.991 |
| Rmerge | 0.101 | 0.064 | 0.753 |
| Number of reflections | 21811 | ||
| <I/σ(I)> | 8.3 | ||
| Completeness [%] | 98.9 | 98 | 90.7 |
| Redundancy | 6.9 | 7 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 1 uL protein (1:10 molar ratio of SETD2:AdoMet) + 1 uL reservoir solution (30% PEG2000 MME, 0.1 M potassium thiocyanate), VAPOR DIFFUSION, HANGING DROP, temperature 298K |
