1E93

High resolution structure and biochemical properties of a recombinant catalase depleted in iron

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-07-15
Spacegroup name	P 62 2 2
Unit cell lengths	108.572, 108.572, 248.760
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 * - 2.000
R-factor	0.199
Rwork	0.199
R-free	0.21500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1CAE
RMSD bond length	0.005
RMSD bond angle	23.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.072 *	0.220 *
Total number of observations	332299 *
Number of reflections	58298
Completeness [%]	97.8 *	94.6
Redundancy	5.7 *	4.4 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	4-5 *	drop was mixed with an equal volume of reservoir solution *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	54 (mg/ml)
2	1	drop	Tris-HCl	100 (mM)
3	1	drop	glycerol	5 (%(v/v))
4	1	reservoir	Tris-HCl	100 (mM)
5	1	reservoir	ammonium sulfate	2 (M)
6	1	reservoir		50 (mM)