1Y25
structure of mycobacterial thiol peroxidase Tpx
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-08-14 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 106.089, 106.089, 65.334 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.770 - 2.100 |
R-factor | 0.17461 |
Rwork | 0.171 |
R-free | 0.24930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1psq |
RMSD bond length | 0.024 |
RMSD bond angle | 2.320 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 92.060 | 2.210 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.048 | 0.260 |
Number of reflections | 24893 | |
<I/σ(I)> | 19.7 | 3.7 |
Completeness [%] | 99.4 | 98.5 |
Redundancy | 3.5 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | ammonium sulfate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K |