1OZR

Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	119
Detector technology	CCD
Collection date	2002-10-17
Detector	ADSC QUANTUM 4
Wavelength(s)	1.000
Spacegroup name	P 1 21 1
Unit cell lengths	61.852, 54.651, 72.141
Unit cell angles	90.00, 99.28, 90.00

Refinement procedure

Resolution	50.000 - 1.740
Rwork	0.209
R-free	0.23200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qq8
RMSD bond length	0.006
RMSD bond angle	1.200
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.800
High resolution limit [Å]	1.740	1.740
Rmerge	0.046 *	0.501 *
Total number of observations	233738 *
Number of reflections	96379 *
<I/σ(I)>	21.1	2.12
Completeness [%]	99.7 *	89.9
Redundancy	9.9	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.4 *	301	ammonium sulphate, 1,6-hexanediol, HEPES, water, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 301K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	2.08 (M)
2	1	reservoir	HEPES	100 (mM)	pH7.5
3	1	reservoir	1,6-hexanediol	0.9 (%(v/v))
4	1	drop	protein	45 (mg/ml)
5	1	drop	potassium phosphate	20 (mM)	pH7.4