1P3T

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	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	119
Detector technology	IMAGE PLATE
Collection date	2002-07-14
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 43 21 2
Unit cell lengths	63.245, 63.245, 102.142
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.100
Rwork	0.254
R-free	0.29700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1j77
RMSD bond length	0.009
RMSD bond angle	1.374 *
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	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.051	0.611
Total number of observations	226194 *
Number of reflections	31166 *
<I/σ(I)>	38.5	2.37
Completeness [%]	96.7 *	97.8
Redundancy	9.5	4.67

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, HANGING 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)