1OZW

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	2002-10-17
Detector	ADSC QUANTUM 4
Wavelength(s)	1.000
Spacegroup name	P 1 21 1
Unit cell lengths	61.681, 54.500, 70.921
Unit cell angles	90.00, 98.81, 90.00

Refinement procedure

Resolution	50.000 - 1.550
Rwork	0.212
R-free	0.23700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qq8
RMSD bond length	0.005
RMSD bond angle	1.100
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	1.610
High resolution limit [Å]	1.550	1.550
Rmerge	0.047 *	0.516 *
Total number of observations	355458 *
Number of reflections	145019 *
<I/σ(I)>	17.3	2.14
Completeness [%]	99.5 *	99.6
Redundancy	9.9	5.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.4 *	301	ammonium sulphate, 1-6 hexane diol, 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