1P3V

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	2002-08-02
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 43 21 2
Unit cell lengths	60.449, 60.449, 102.361
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.250
Rwork	0.249
R-free	0.28600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1j77
RMSD bond length	0.011
RMSD bond angle	1.402
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	2.330
High resolution limit [Å]	2.250	2.250
Rmerge	0.054	0.540
Total number of observations	123533 *
Number of reflections	26432 *
<I/σ(I)>	21.3	2.39
Completeness [%]	89.7 *	89.8
Redundancy	9.5	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	295	Tris-HCl, sodium acetate, PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K

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)