1OAH

Cytochrome c Nitrite Reductase from Desulfovibrio desulfuricans ATCC 27774: The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA).

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-05-15
Detector	MARRESEARCH
Wavelength(s)	1.7403,1.7390,0.9919, 0.932
Spacegroup name	P 21 21 21
Unit cell lengths	78.940, 104.600, 143.180
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.300
Rwork	0.189
R-free	0.22400
Structure solution method	MAD AND MR
Starting model (for MR)	1qdb
RMSD bond length	0.008 *
RMSD bond angle	1.378 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.080	0.390
Number of reflections	51633 *
<I/σ(I)>	11.7	2.2
Completeness [%]	97.3 *	89.8
Redundancy	5.6	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5		15% W/V PEG 3350, CACL2 0.2M, HEPES PH7.5, 0.1M, 3-(DECYL-METHYLAMMONIUM)PROPANE-1-SULFONATE (ZWITTERGENT 3-10) AS ADDITIVE, pH 7.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG3350	15 (%(w/v))
2	1	reservoir		0.2 (M)
3	1	reservoir	HEPES	0.1 (M)	pH7.5
4	1	drop	protein	10 (mg/ml)