1OZL

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 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	119
Detector technology	CCD
Collection date	2002-10-14
Detector	ADSC QUANTUM 4
Wavelength(s)	1.000
Spacegroup name	P 1 21 1
Unit cell lengths	61.435, 54.415, 71.004
Unit cell angles	90.00, 99.23, 90.00

Refinement procedure

Resolution	50.000 - 1.580
Rwork	0.205
R-free	0.22200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qq8
RMSD bond length	0.007
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	1.640
High resolution limit [Å]	1.580	1.580
Rmerge	0.038 *	0.401 *
Total number of observations	208425 *
Number of reflections	63001 *
<I/σ(I)>	18.2	2.14
Completeness [%]	99.1 *	94.2
Redundancy	9.1	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.4 *	301	ammomium 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