4U9B
Crystal structure of an H-NOX protein from S. oneidensis in the Fe(II)NO ligation state
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-07-07 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.11 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 67.636, 86.716, 33.822 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.818 - 1.650 |
R-factor | 0.1693 |
Rwork | 0.168 |
R-free | 0.20270 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4u99 |
RMSD bond length | 0.019 |
RMSD bond angle | 0.864 |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.818 | 1.740 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.029 | 0.487 |
Number of reflections | 45550 | |
<I/σ(I)> | 14.4 | 1.7 |
Completeness [%] | 98.5 | 99.5 |
Redundancy | 3.9 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | Obtained by equilibrating a 2 or 4 uL drop of 1:1 protein: reservoir against 700 uL reservoir containing 0.7 M NaH2PO4, 0.9 M K2HPO4. Cryoprotection was achieved by carefully adding equal drop volume of mother liquor containing 50% glycerol. Crystals were then transferred into mother liquor containing 30% glycerol and flash frozen in liquid nitrogen. All crystal growth and manipulation was performed anaerobically. |