8QQ5
Structure of WT SpNox DH domain: a bacterial NADPH oxidase.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-1 |
Synchrotron site | ESRF |
Beamline | MASSIF-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-09-10 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.966 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 104.880, 104.880, 139.290 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.900 - 2.500 |
R-factor | 0.2014 |
Rwork | 0.197 |
R-free | 0.28960 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.456 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.900 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 26155 | 2978 |
<I/σ(I)> | 18.99 | |
Completeness [%] | 100.0 | |
Redundancy | 25.96 | |
CC(1/2) | 0.999 | 0.639 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | Protein: 15 mg/ml in 100 mM bis-TRIS propane pH 6.5, 300 mM NaCl, 5% glycerol, 0.01 mM FAD. Crystallization condition: 35% PEG MME 500 and 0.1 M sodium citrate pH5. Drop: 100 nL of protein +100 nL of well. |