5AO3
Crystal structure of human SAMHD1 (amino acid residues 115-626) bound to GTP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Detector | DECTRIS PILATUS |
Spacegroup name | P 1 |
Unit cell lengths | 81.919, 95.733, 97.592 |
Unit cell angles | 91.37, 108.97, 115.33 |
Refinement procedure
Resolution | 29.657 - 3.004 |
R-factor | 0.1807 |
Rwork | 0.177 |
R-free | 0.24730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3u1n |
RMSD bond length | 0.010 |
RMSD bond angle | 1.338 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX ((PHENIX.REFINE: 1.8.4_1496)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.180 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.060 | 0.410 |
Number of reflections | 45153 | |
<I/σ(I)> | 10.52 | 1.9 |
Completeness [%] | 90.9 | 83.1 |
Redundancy | 1.73 | 1.69 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.2 M AMMONIUM SULPHATE, 20% PEG 3350 |