7DAO
Crystal structure of native yak lactoperoxidase at 2.28 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-10-08 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9677 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 80.162, 85.242, 96.443 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.620 - 2.280 |
Rwork | 0.174 |
R-free | 0.24340 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7d52 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.533 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.621 | 2.340 |
High resolution limit [Å] | 2.280 | 2.280 |
Rmerge | 0.150 | |
Rmeas | 0.990 | |
Number of reflections | 30344 | 2081 |
<I/σ(I)> | 7 | 2.28 |
Completeness [%] | 99.0 | 93 |
Redundancy | 7 | |
CC(1/2) | 0.990 | 0.790 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 0.05M potassium fluoride, 20% PEG 3350 |