1MY6

The 1.6 A Structure of Fe-Superoxide Dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus : Correlation of EPR and Structural Characteristics

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X8C
Synchrotron site	NSLS
Beamline	X8C
Temperature [K]	100
Detector technology	CCD
Collection date	2002-06-02
Detector	ADSC QUANTUM 4
Wavelength(s)	1.100
Spacegroup name	P 1 21 1
Unit cell lengths	51.749, 63.644, 74.709
Unit cell angles	90.00, 110.45, 90.00

Refinement procedure

Resolution	70.000 - 1.600
R-factor	0.19577
Rwork	0.194
R-free	0.22600 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	FeSOD from E.coli PDB entry 1isc
RMSD bond length	0.018 *
RMSD bond angle	2.000 *
Phasing software	EPMR
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	70.000	1.642
High resolution limit [Å]	1.600	1.600
Rmerge	0.088 *	0.322 *
Total number of observations	274614 *
Number of reflections	53851
<I/σ(I)>	6.35	6.35
Completeness [%]	99.6 *	94.5 *
Redundancy	16.18	14.28

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	293.15	VAPOR DIFFUSION, HANGING DROP, 293.15K, 0.1M Sodium Cacodylate pH 6.7, 0.2M Magnesium Acetate Tetrahydrate, 20% PEG 6K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	11.7 (mg/ml)
2	1	drop	Tris	10 (mM)	pH7.5
3	1	reservoir	sodium cacodylate	0.1 (M)	pH6.7
4	1	reservoir	magnesium acetate tetrahydrate	0.2 (M)
5	1	reservoir	PEG6000	20 (%)