5B72
Crystal structure of bovine lactoperoxidase with a broken covalent bond between Glu258 and heme moiety at 1.98 A resolution.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 291 |
| Detector technology | CCD |
| Collection date | 2015-09-30 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.847, 80.192, 75.086 |
| Unit cell angles | 90.00, 105.41, 90.00 |
Refinement procedure
| Resolution | 72.390 - 1.980 |
| R-factor | 0.18993 |
| Rwork | 0.188 |
| R-free | 0.23508 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4S0Y |
| RMSD bond length | 0.017 |
| RMSD bond angle | 2.062 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 72.390 | 2.010 |
| High resolution limit [Å] | 1.980 | 1.980 |
| Rmerge | 0.660 | |
| Number of reflections | 41631 | |
| <I/σ(I)> | 11.5 | 1.1 |
| Completeness [%] | 96.7 | 69.1 |
| Redundancy | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 298 | 0.2M AMMONIUM IODIDE, 20% PEG3350, pH 6.8, VAPOR DIFFUSION, HANGING DROP, 298K. |
