6O5W
Crystal structure of MORC3 CW domain fused with viral influenza A NS1 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2017-08-11 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.28 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 30.912, 37.424, 50.314 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 26.338 - 1.412 |
R-factor | 0.1544 |
Rwork | 0.153 |
R-free | 0.16870 |
Structure solution method | SAD |
Starting model (for MR) | 5svx |
RMSD bond length | 0.005 |
RMSD bond angle | 0.948 |
Data reduction software | HKL-3000 |
Data scaling software | SCALEPACK |
Phasing software | AutoSol |
Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.430 |
High resolution limit [Å] | 1.410 | 1.410 |
Number of reflections | 71940 | 554 |
<I/σ(I)> | 92.4 | |
Completeness [%] | 99.2 | |
Redundancy | 11 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 289.15 | 100 mM HEPES pH 7.5 and 1.4M Sodium Citrate |