3ERH
First structural evidence of substrate specificity in mammalian peroxidases: Crystal structures of substrate complexes with lactoperoxidases from two different species
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 291 |
Detector technology | IMAGE PLATE |
Collection date | 2008-09-24 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.54132 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.207, 80.541, 77.877 |
Unit cell angles | 90.00, 102.64, 90.00 |
Refinement procedure
Resolution | 19.460 - 2.400 |
R-factor | 0.18 |
Rwork | 0.180 |
R-free | 0.19500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2r5l |
RMSD bond length | 0.007 |
RMSD bond angle | 1.700 |
Data reduction software | AUTOMAR |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.460 | 2.500 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 25355 | |
Completeness [%] | 98.6 | 99.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 10mM Phosphate buffre, 2mM CaCl2, 20% PEG3350, 0.2M Ammonium Iodide, pH6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |