1AR4

X-RAY STRUCTURE ANALYSIS OF THE CAMBIALISTIC SUPEROXIDE DISMUTASE FROM PROPIONIBACTERIUM SHERMANII ACTIVE WITH FE OR MN

Experimental procedure

Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR591
Temperature [K]	295
Detector technology	AREA DETECTOR
Collection date	1997-12
Detector	SIEMENS HI-STAR
Spacegroup name	C 2 2 21
Unit cell lengths	79.680, 85.640, 108.850
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	9.000 - 1.900
R-factor	0.156
Rwork	0.156
R-free	0.20500
Structure solution method	ISOMORPHOUS WITH FE-SOD OF P.SHERMANII
Starting model (for MR)	FE-SOD OF P.SHERMANII
RMSD bond length	0.005
RMSD bond angle	21.840 *
Data reduction software	SAINT
Data scaling software	CCP4 ((AGROVATA)
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	12.800	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.042	0.042
Total number of observations	81457 *
Number of reflections	26323
<I/σ(I)>	17	5.3
Completeness [%]	89.2	72.3
Redundancy	3.1	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.1	4 *	PROTEIN WAS CRYSTALLIZED AT 50MG/ML FROM 2.15 M (NH4)2SO4, 50 MM KPI, PH 6.15, 4 DEG C, NUCLEATION INDUCED BY MICROSEEDING FROM CRYSTALS GROWN FROM 14MG/ML PROTEIN, 2.4 M (NH4)2SO4, 50 MM KPI, PH 7.4, 4 DEG C., microseeding, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	50 (mg/ml)
2	1	drop	ammonium sulfate	2.15 (M)