6H1Y
CRYSTAL STRUCTURE OF A CHIMERIC VARIANT OF THIOREDOXIN FROM ESCHERICHIA COLI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-02-19 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.54 |
Spacegroup name | P 31 |
Unit cell lengths | 95.340, 95.340, 39.646 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 82.570 - 2.990 |
R-factor | 0.20583 |
Rwork | 0.198 |
R-free | 0.25945 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2trx |
RMSD bond length | 0.011 |
RMSD bond angle | 1.496 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 82.570 | 3.130 |
High resolution limit [Å] | 2.990 | 2.990 |
Rmerge | 0.079 | |
Number of reflections | 7669 | |
<I/σ(I)> | 14.8 | |
Completeness [%] | 93.6 | |
Redundancy | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | Crystals were obtained with a protein concentration of 20-25 mg/ml. The composition of the reservoir solution was 17% (w/v) PEG10000, 0.1 M ammonium acetate and 0.1 M BIS-TRIS buffer, pH 5.5. |