2VPS
Structure Of The Bifunctional Leishmania Major Trypanothione Synthetase-Amidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-09-19 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 71.050, 85.600, 168.340 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.330 - 2.750 |
| R-factor | 0.207 |
| Rwork | 0.204 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vob |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.464 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.900 |
| High resolution limit [Å] | 2.750 | 2.750 |
| Rmerge | 0.090 | 0.460 |
| Number of reflections | 96640 | |
| <I/σ(I)> | 21.7 | 3.5 |
| Completeness [%] | 96.5 | 88.6 |
| Redundancy | 3.5 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
