3TUE
The structure of tryparedoxin peroxidase I from Leishmania major
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Detector technology | CCD |
Collection date | 2011-03-18 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.91841 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 112.977, 212.385, 90.948 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 106.000 - 3.000 |
R-factor | 0.19889 |
Rwork | 0.197 |
R-free | 0.23342 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1e2y |
RMSD bond length | 0.005 |
RMSD bond angle | 1.020 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 106.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Number of reflections | 21162 | |
<I/σ(I)> | 7.3 | 1.84 |
Completeness [%] | 99.9 | 99.2 |
Redundancy | 2.9 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 22% PEG 3350, 0.1 M BIS-TRIS PROPANE, 0.2 M KSCN, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |