1AOG
TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE (OXIDIZED FORM)
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1991-03 |
Detector | RIGAKU RAXIS |
Spacegroup name | P 43 |
Unit cell lengths | 92.810, 92.810, 156.690 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.300 |
R-factor | 0.189 |
Rwork | 0.189 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tyt |
RMSD bond length | 0.010 |
RMSD bond angle | 24.100 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 2.300 | 2.300 * |
Rmerge | 0.109 | |
Total number of observations | 170106 * | |
Number of reflections | 55392 | |
Completeness [%] | 94.1 | 80 * |
Redundancy | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 | 6-8 * | pH 6.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7.5 (mg/ml) | |
2 | 1 | drop | maleic acid | 100 (mM) | |
3 | 1 | drop | dioxane | 0.2 (%(v/v)) | |
4 | 1 | drop | sodium dihydrogen phosphate | 1 (%) | |
5 | 1 | drop | PEG8000 | 10 (%) | |
6 | 1 | reservoir | PEG8000 | 20 (%) |