4U9G
Crystal structure of an H-NOX protein from S. oneidensis in the Fe(II)CO ligation state, Q154A/Q155A/K156A mutant
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 | 2014-01-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.00 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 164.173, 164.173, 102.366 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.010 - 2.250 |
R-factor | 0.182 |
Rwork | 0.182 |
R-free | 0.19300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4u99 |
RMSD bond length | 0.009 |
RMSD bond angle | 0.887 |
Refinement software | PHENIX ((PHENIX.REFINE: 1.9_1692)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.007 | 2.320 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.028 | 0.446 |
Number of reflections | 70856 | |
<I/σ(I)> | 20.2 | 1.8 |
Completeness [%] | 96.7 | 98.1 |
Redundancy | 11.1 | 11.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.3 | 293 | OBTAINED BY EQUILIBRATING A 2 UL DROP OF 1:1 PROTEIN:RESERVOIR AGAINST A 700 UL RESERVOIR CONTAINING 1.6-1.9 M DL-MALIC ACID (PH 7.3). FOR CRYOPROTECTION, 2 UL OF MOTHER LIQUOR CONTAINING 10% GLYCEROL WAS ADDED DIRECTLY TO THE DROP AND CRYSTALS WERE SERIAL TRANSFERRED INTO MOTHER LIQUOR SOLUTION CONTAINING 5, 7.5 AND 10% GLYCEROL. PRIOR TO FLASH FREEZING IN LIQUID NITROGEN, CRYSTALS WERE TRANSFERRED UNDER A LAYER OF OIL AND INCUBATED WITH CARBON MONOXIDE-SATURATED CRYOPROTECTANT FOR 15-45 MINUTES. CRYSTAL GROWTH AND MANIPULATION WAS PERFORMED ANAEROBICALLY. |