1EWX
Crystal structure of native tryparedoxin I from Crithidia fasciculata
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-07-06 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.940, 51.390, 71.460 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.900 - 1.700 |
R-factor | 0.168 |
Rwork | 0.168 |
R-free | 0.21300 * |
RMSD bond length | 0.021 |
RMSD bond angle | 0.036 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.200 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.073 | 0.089 |
Number of reflections | 15563 | |
<I/σ(I)> | 5.9 | |
Completeness [%] | 97.9 | 100 |
Redundancy | 3.2 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.7 | 294 * | Kalisz, H.M., (1998) Acta Crystallogr., Sect.D, 55, 696. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 13.5 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 33 (%(w/w)) | |
3 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.7 |
4 | 1 | reservoir | sodium acetate | 50 (mM) |