5ZG4
Crystal Structure of Triosephosphate isomerase SAD deletion mutant from Opisthorchis viverrini
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2016-10-26 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.900000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 73.742, 91.924, 75.775 |
| Unit cell angles | 90.00, 109.13, 90.00 |
Refinement procedure
| Resolution | 36.360 - 1.746 |
| R-factor | 0.1616 |
| Rwork | 0.160 |
| R-free | 0.19260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5zfx |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.112 |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 45.960 | 45.960 | 1.780 |
| High resolution limit [Å] | 1.750 | 9.560 | 1.750 |
| Rmerge | 0.075 | 0.023 | 0.495 |
| Rmeas | 0.085 | 0.027 | 0.568 |
| Rpim | 0.041 | 0.013 | 0.276 |
| Total number of observations | 410025 | 2429 | 19219 |
| Number of reflections | 96733 | 615 | 4711 |
| <I/σ(I)> | 14.1 | 36.8 | 2.8 |
| Completeness [%] | 99.8 | 98.4 | 97.8 |
| Redundancy | 4.2 | 3.9 | 4.1 |
| CC(1/2) | 0.998 | 0.999 | 0.840 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 8.5 | 293 | PEG 3350 |
