1ITK

Crystal structure of catalase-peroxidase from Haloarcula marismortui

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-6A
Synchrotron site	Photon Factory
Beamline	BL-6A
Temperature [K]	100
Detector technology	CCD
Collection date	2001-01-25
Detector	ADSC QUANTUM 4
Wavelength(s)	1.000
Spacegroup name	C 1 2 1
Unit cell lengths	317.632, 82.141, 75.102
Unit cell angles	90.00, 100.24, 90.00

Refinement procedure

Resolution	34.100 - 2.000
Rwork	0.182
R-free	0.20500 *
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	1.620 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	MLPHARE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.100 *	2.110
High resolution limit [Å]	2.000	2.000
Rmerge	0.052	0.140
Total number of observations	479060 *
Number of reflections	128391	18662 *
<I/σ(I)>	9.3	5
Completeness [%]	99.9	99.7
Redundancy	3.7	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	20 *	ammonium sulfate, potassium chloride, Tris/HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	40-50 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)	pH8.0
3	1	drop	ammonium sulfate	2.0 (M)
4	1	drop		0.5 (M)
5	1	reservoir	ammonium sulfate	3.0-3.2 (M)