2PT3
Crystal structure of bovine lactoperoxidase at 2.34 A resolution reveals multiple anion binding sites
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 200 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-10-20 |
| Detector | MAR scanner 345 mm plate |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.910, 80.051, 75.675 |
| Unit cell angles | 90.00, 103.23, 90.00 |
Refinement procedure
| Resolution | 19.380 - 2.340 |
| R-factor | 0.2319 |
| Rwork | 0.231 |
| R-free | 0.24682 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2nqx |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.075 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 74.700 | 2.380 |
| High resolution limit [Å] | 2.340 | 2.340 |
| Number of reflections | 24867 | |
| <I/σ(I)> | 26.5 | |
| Completeness [%] | 98.5 | 99.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.8 | 298 | Tris-HCl, Phosphate, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
