5JRU
Crystal structure of Fe(II) unliganded H-NOX protein from C. subterraneus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2014-11-01 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.99994 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 86.264, 70.446, 108.419 |
Unit cell angles | 90.00, 104.93, 90.00 |
Refinement procedure
Resolution | 44.919 - 2.305 |
R-factor | 0.1938 |
Rwork | 0.192 |
R-free | 0.25440 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3lah |
RMSD bond length | 0.014 |
RMSD bond angle | 1.646 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.920 | 2.340 |
High resolution limit [Å] | 2.300 | 2.300 |
Number of reflections | 55562 | |
<I/σ(I)> | 17.12 | 4.8 |
Completeness [%] | 99.7 | 96.5 |
Redundancy | 2.01 | |
CC(1/2) | 0.968 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | Anaerobically grown under Argon. 30 mg/mL protein with well condition of 0.1 M NaI, 22% PEG 3350. |