5ALA
Structure of Leishmania major peroxidase D211R mutant (low res)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-09-20 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.880, 79.170, 179.190 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.837 - 2.730 |
| R-factor | 0.2127 |
| Rwork | 0.209 |
| R-free | 0.28230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3riv |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.277 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.690 | 2.830 |
| High resolution limit [Å] | 2.730 | 2.730 |
| Rmerge | 0.850 | 1.290 |
| Number of reflections | 18116 | |
| <I/σ(I)> | 18.5 | 1.4 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 3.9 | 4.1 |
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 |
