3TF0
Crystal structure of an H-NOX protein from T. tengcongensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-05-23 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.977 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 80.502, 130.766, 42.736 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.470 - 1.743 |
| R-factor | 0.2034 |
| Rwork | 0.202 |
| R-free | 0.22940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1u4h |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.992 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7_650)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.800 |
| High resolution limit [Å] | 1.743 | 1.743 |
| Number of reflections | 43735 | |
| Completeness [%] | 93.1 | 90.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 20-28% PEG 2000, 200-250 mM Sodium Acetate (pH 7.5), VAPOR DIFFUSION, SITTING DROP, temperature 293K |






