6D66
Crystal structure of the human dual specificity 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein mbp3_16
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-05-11 |
Detector | MARRESEARCH |
Wavelength(s) | 1.54 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 79.967, 79.967, 265.797 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.444 - 2.226 |
R-factor | 0.1615 |
Rwork | 0.159 |
R-free | 0.20180 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6d65 |
RMSD bond length | 0.007 |
RMSD bond angle | 0.777 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.300 |
High resolution limit [Å] | 2.220 | 2.220 |
Rmerge | 0.050 | 0.388 |
Number of reflections | 43247 | 3697 |
<I/σ(I)> | 46.4 | 3.6 |
Completeness [%] | 98.6 | 86.5 |
Redundancy | 10.7 | 7.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 292 | 0.2 M DL-glutamic acid 0.2 M DL-alanine 0.2 M -glycine 0.2 M-DL-lysine 0.2 M DL-serine 0.1 M Tris: Bicine 25% MPD 25% PEG1000 25% PEG3350 |