5WV3
Crystal structure of bovine lactoperoxidase with a partial Glu258-heme linkage at 2.07 A resolution.
Replaces: 5K1EExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-26 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.012, 79.809, 66.106 |
| Unit cell angles | 90.00, 93.01, 90.00 |
Refinement procedure
| Resolution | 34.170 - 2.070 |
| R-factor | 0.16918 |
| Rwork | 0.167 |
| R-free | 0.23601 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5K1E |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.298 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 66.010 | 2.110 |
| High resolution limit [Å] | 2.070 | 2.070 |
| Number of reflections | 32253 | |
| <I/σ(I)> | 17.3 | 2.3 |
| Completeness [%] | 94.6 | 69.1 |
| Redundancy | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | NaNO3, PEG3350, pH6.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
