4F82
X-ray crystal structure of a putative thioredoxin reductase from Burkholderia cenocepacia
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-05-12 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.977408 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 37.650, 61.970, 69.810 |
Unit cell angles | 90.00, 98.85, 90.00 |
Refinement procedure
Resolution | 46.099 - 1.850 |
R-factor | 0.178 |
Rwork | 0.176 |
R-free | 0.22350 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tp9 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.524 |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (dev_1048) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.900 | |
High resolution limit [Å] | 1.850 | 8.270 | 1.850 |
Rmerge | 0.117 | 0.042 | 0.400 |
Number of reflections | 26023 | 274 | 1948 |
<I/σ(I)> | 6.36 | 16.71 | 2.23 |
Completeness [%] | 95.5 | 82.5 | 95.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 289 | 200 mM magnesium chloride, 25% PEG3350, 100 BIS-TRIS pH 5.50, VAPOR DIFFUSION, SITTING DROP, temperature 289K |