5AMM
Structure of Leishmania major peroxidase D211N mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 12.3.1 |
Synchrotron site | ALS |
Beamline | 12.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-10-10 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.249, 78.310, 160.977 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.090 |
R-factor | 0.18717 |
Rwork | 0.184 |
R-free | 0.24455 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3riv |
RMSD bond length | 0.014 |
RMSD bond angle | 1.704 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.170 |
High resolution limit [Å] | 2.090 | 2.090 |
Rmerge | 0.030 | 0.550 |
Number of reflections | 34997 | |
<I/σ(I)> | 18.69 | 1.35 |
Completeness [%] | 99.2 | 94.9 |
Redundancy | 2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 10% PEG MME 5000, 0.1M MES:NAOH PH 6.5, 7.5 MM PRASEODYMIUM(III) ACETATE HYDRATE |