8TDR
Crystal structure of the methyltransferase domain of DNMT3A homotetramer
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-02-07 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1 |
Spacegroup name | P 3 |
Unit cell lengths | 179.429, 179.429, 108.065 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 46.290 - 3.320 |
R-factor | 0.2108 |
Rwork | 0.210 |
R-free | 0.23960 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5yx2 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 3.440 |
High resolution limit [Å] | 3.320 | 7.150 | 3.320 |
Rmerge | 0.220 | 0.042 | 1.319 |
Rmeas | 0.254 | 0.049 | 1.538 |
Rpim | 0.127 | 0.024 | 0.782 |
Total number of observations | 225061 | ||
Number of reflections | 57297 | 5722 | 5689 |
<I/σ(I)> | 3.3 | ||
Completeness [%] | 100.0 | 99.8 | 100 |
Redundancy | 3.9 | 4.1 | 3.7 |
CC(1/2) | 0.998 | 0.834 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.2-0.4 M potassium sodium tartrate |