3BO5
Crystal structure of methyltransferase domain of human Histone-lysine N-methyltransferase SETMAR
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-12-05 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9793143, 1.2832396 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 41.396, 67.827, 44.637 |
Unit cell angles | 90.00, 105.93, 90.00 |
Refinement procedure
Resolution | 42.910 - 1.590 |
R-factor | 0.15741 |
Rwork | 0.155 |
R-free | 0.19889 |
Structure solution method | MAD |
RMSD bond length | 0.021 |
RMSD bond angle | 2.057 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | SHELXD |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.910 | 1.660 |
High resolution limit [Å] | 1.590 | 1.590 |
Number of reflections | 31726 | |
<I/σ(I)> | 27 | 2.5 |
Completeness [%] | 99.8 | 98.5 |
Redundancy | 4.9 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 25% PEG 3350, 0.2 M Ammonium acetate, 0.1 M Bis-Tris pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |