1P3U

Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis: Implications for Oxygen Activation

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	2002-07-17
Detector	ADSC QUANTUM 4
Spacegroup name	P 43 21 2
Unit cell lengths	63.033, 63.033, 101.105
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.750
Rwork	0.252
R-free	0.28700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1j77
RMSD bond length	0.009
RMSD bond angle	1.323
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	1.810
High resolution limit [Å]	1.750	1.750
Rmerge	0.035	0.541
Total number of observations	85041 *
Number of reflections	34991 *
<I/σ(I)>	27.3	4.6
Completeness [%]	86.9 *	90.1 *
Redundancy	9.6	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	298	tris-HCl, sodium acetate, PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	Tris-HCl	0.1 (M)	pH8.5
2	1	reservoir	sodium acetate	0.2 (M)
3	1	reservoir	PEG3350	32.5 (%)
4	1	drop	protein	23 (mg/ml)