1AR5

X-RAY STRUCTURE 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	1995-11
Detector	SIEMENS
Spacegroup name	C 2 2 21
Unit cell lengths	79.830, 85.687, 108.590
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.600
R-factor	0.163
Rwork	0.163
R-free	0.18400
Structure solution method	MR/MIR
Starting model (for MR)	FE-SOD E.COLI MN-SOD T.THERMOPHILUS
RMSD bond length	0.005
RMSD bond angle	21.006 *
Data reduction software	SAINT
Data scaling software	Agrovata
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	39.800	1.660
High resolution limit [Å]	1.600	1.600
Rmerge	0.034 *	0.136
Total number of observations	119504 *
Number of reflections	47484
<I/σ(I)>	22.7	7
Completeness [%]	85.6 *	72.7 *
Redundancy	3.9	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.1 *	4 *	PROTEIN WAS CRYSTALLIZED FROM 2.15 M (NH4)2SO4, 50 MM KPI, PH 6.15 AT 4 DEG C. NUCLEATION WAS INDUCED BY ADDING A MICROSEED FROM CRYSTALS GROWN FROM 2.4 M (NH4)2SO4, 50MM KPI, PH 7.4 AT 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)