5AL9
Structure of Leishmania major peroxidase D211R mutant (high res)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-08-24 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 142.439, 57.860, 36.620 |
| Unit cell angles | 90.00, 97.59, 90.00 |
Refinement procedure
| Resolution | 36.511 - 1.370 |
| R-factor | 0.1858 |
| Rwork | 0.185 |
| R-free | 0.20370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3riv |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.118 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.540 | 1.440 |
| High resolution limit [Å] | 1.370 | 1.370 |
| Rmerge | 0.100 | 0.900 |
| Number of reflections | 61602 | |
| <I/σ(I)> | 5.7 | 1.5 |
| Completeness [%] | 98.1 | 98.1 |
| Redundancy | 2.5 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 10% PEG MME 5000, 0.1M MES:NAOH PH 6.5, 5% DMSO, 7.5 MM PRASEODIMIUM(III) ACETATE HYDRATE |
