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 |
