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 |
