5ZFX
Crystal Structure of Triosephosphate isomerase from Opisthorchis viverrini
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 5C (4A) |
Synchrotron site | PAL/PLS |
Beamline | 5C (4A) |
Temperature [K] | 273 |
Detector technology | CCD |
Collection date | 2013-11-06 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.00001 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 96.529, 206.621, 97.466 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.075 - 1.751 |
R-factor | 0.1648 |
Rwork | 0.164 |
R-free | 0.20040 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tph |
RMSD bond length | 0.007 |
RMSD bond angle | 0.929 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.810 |
High resolution limit [Å] | 1.750 | 3.770 | 1.750 |
Rmerge | 0.105 | 0.114 | 0.110 |
Total number of observations | 541897 | ||
Number of reflections | 96825 | 10127 | 9052 |
<I/σ(I)> | 37.7 | ||
Completeness [%] | 98.8 | 99.6 | 93.3 |
Redundancy | 5.6 | 8.7 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 8.5 | 293 | PEG 3350 |