3ERI

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	2008-09-05
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.54132
Spacegroup name	P 1 21 1
Unit cell lengths	54.537, 80.592, 77.832
Unit cell angles	90.00, 102.63, 90.00

Refinement procedure

Resolution	19.480 - 2.500
R-factor	0.1809
Rwork	0.181
R-free	0.20120
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2r5l
RMSD bond length	0.009
RMSD bond angle	1.900
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]	19.480	2.600
High resolution limit [Å]	2.500	2.500
Number of reflections	21599
Completeness [%]	94.5	96

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	298	10mM phosphate buffer, 2mM CaCl2, 0.2M ammonium Iodide, 20% PEG3350, pH6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K