4WOD
The duplicated taurocyamine kinase from Schistosoma mansoni complexed with arginine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-10-29 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.920, 123.070, 62.740 |
| Unit cell angles | 90.00, 108.07, 90.00 |
Refinement procedure
| Resolution | 45.813 - 1.900 |
| R-factor | 0.2079 |
| Rwork | 0.206 |
| R-free | 0.25120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4wo8 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.106 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 58275 | |
| <I/σ(I)> | 12.11 | 3.41 |
| Completeness [%] | 98.9 | 96.2 |
| Redundancy | 4.2 | 3.7 |
| CC(1/2) | 0.993 | 0.892 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 200 mM ammonium tartrate dibasic pH 5.4, 20% (w/v) polyethylene glycol 3350, 20% (v/v) ethylene glycol, 5 mM L-Arginine |
