1E85

Cytochrome c' from Alcaligenes xylosoxidans - reduced structure with NO bound to proximal side of heme

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-01-15
Detector	ADSC CCD
Spacegroup name	P 65 2 2
Unit cell lengths	53.035, 53.035, 180.993
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.000 - 1.350
R-factor	0.194 *
Rwork	0.194
R-free	0.22000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cgo
RMSD bond length	0.011
RMSD bond angle	0.024
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	1.370
High resolution limit [Å]	1.350	1.350
Rmerge	0.039	0.227
Number of reflections	33925
<I/σ(I)>	39.8	3.9
Completeness [%]	98.8	93.1
Redundancy	6.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2 *	4 *	HANGING DROP VAPOUR DIFFUSION. PROTEIN AT CONCENTRATION 8 MG/ML WAS MIXED WITH AN EQUAL VOLUME OF WELL SOLUTION CONSISTING OF 55-65% SATURATED AMMONIUM SULFATE IN 100 MM HEPES BUFFER AT PH 7.5. REDUCED USING MOTHER LIQUOR CONTAINING 20 MM SODIUM DITHIONITE, THEN INCUBATED FOR 6 DAYS IN MOTHER LIQUOR SATURATED WITH NO.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)
3	1	reservoir	ammonium sulfate	55-65 (%sat)
4	1	reservoir	HEPES	100 (mM)