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 |