3GCJ
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 | 2008-10-20 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.54312 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.618, 80.553, 77.803 |
Unit cell angles | 90.00, 102.55, 90.00 |
Refinement procedure
Resolution | 19.470 - 2.340 |
R-factor | 0.204 |
Rwork | 0.204 |
R-free | 0.21200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3bxi |
RMSD bond length | 0.009 |
RMSD bond angle | 1.700 |
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] | 19.470 | 2.400 |
High resolution limit [Å] | 2.340 | 2.340 |
Number of reflections | 27438 | |
Completeness [%] | 98.5 | 95.2 |
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 |