1LY8

The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-04-27
Detector	MARRESEARCH
Wavelength(s)	1.08535
Spacegroup name	P 21 21 2
Unit cell lengths	74.490, 114.860, 73.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.910 - 2.050
R-factor	0.202
Rwork	0.202
R-free	0.24900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	21.800 *
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]	20.000	2.100
High resolution limit [Å]	2.050	2.050
Rmerge	0.086	0.186
Total number of observations	110655 *
Number of reflections	35855
Completeness [%]	91.6 *	89.4 *
Redundancy	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	5.5 *	277	1.6M ammonium sulphate, 0.1M 2-(N- Morpholino)ethanesulfonic acid, pH 6.2, VAPOR DIFFUSION, HANGING DROP at 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	ammonium sulfate	1.5 (M)
2	1	drop	sodium acetate	0.1 (M)	pH5.5
3	1	reservoir	MES	0.1 (M)	pH6.2
4	1	reservoir	ammonium sulfate	1.6 (M)