3TF1
Crystal structure of an H-NOX protein from T. tengcongensis under 6 atm of xenon
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 | 2010-05-30 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.23 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 80.128, 130.214, 42.810 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.810 - 2.037 |
R-factor | 0.1818 |
Rwork | 0.180 |
R-free | 0.22100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3tf0 |
RMSD bond length | 0.018 |
RMSD bond angle | 1.517 |
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 | 2.070 |
High resolution limit [Å] | 2.030 | 2.030 |
Number of reflections | 52373 | |
Completeness [%] | 94.7 | 99.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 20-28% PEG 200, 200-250 mM Sodium Acetate pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |