5HT6
Crystal structure of the SET domain of the human MLL5 methyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-07-18 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.07245 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 65.900, 65.900, 112.900 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.933 - 2.093 |
R-factor | 0.2116 |
Rwork | 0.209 |
R-free | 0.24240 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.841 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.21) |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 57.174 | 2.210 |
High resolution limit [Å] | 2.093 | 2.100 |
Rmerge | 0.390 | |
Number of reflections | 17289 | |
<I/σ(I)> | 22 | 2 |
Completeness [%] | 99.9 | 99.7 |
Redundancy | 8 | 8.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2M NH4Cl, 12 % (w/v) PEG 3350 |