3GCL
Mode of ligand binding and assignment of subsites in mammalian peroxidases: crystal structure of lactoperoxidase complexes with acetyl salycylic acid, salicylhydroxamic acid and benzylhydroxamic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 291 |
| Detector technology | IMAGE PLATE |
| Collection date | 2008-06-27 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.54312 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.660, 80.520, 77.970 |
| Unit cell angles | 90.00, 102.65, 90.00 |
Refinement procedure
| Resolution | 19.440 - 2.500 |
| R-factor | 0.201 |
| Rwork | 0.201 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bxi |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.440 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Number of reflections | 22613 | |
| Completeness [%] | 98.9 | 95.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 298 | 0.2M ammonium iodide, 20% PEG3350, pH6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
