1VEW

MANGANESE SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU FR-C
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-07
Detector	RIGAKU
Spacegroup name	C 2 2 21
Unit cell lengths	100.840, 108.910, 182.100
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.100
R-factor	0.186
Rwork	0.188
R-free	0.21800 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1mng
RMSD bond length	0.010
RMSD bond angle	15.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	TNT (5E)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.200
High resolution limit [Å]	2.100	2.100
Rmerge	0.056 *	0.191 *
Total number of observations	215051 *
Number of reflections	56890
<I/σ(I)>	22	5.4
Completeness [%]	96.8	77
Redundancy	3.7	0.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5		CRYSTALS WERE GROWN AT ROOM TEMPERATURE USING THE HANGING DROP METHOD. THE HANGING DROPS WERE SUSPENDED OVER 0.75ML OF WELL SOLUTION (16-30% PEG6000 AND 0.05M BICINE TITRATED TO PH8.5) AND CONSISTED OF 2UL OF WELL SOLUTION AND 2UL OF PROTEIN SOLUTION (MNSOD AT 12MG/ML IN WATER)., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	drop	PEG6000	8-15 (%)
3	1	drop	bicine titrated	0.025 (M)
4	1	reservoir	PEG6000	16-30 (%)
5	1	reservoir	bicine titrated	0.05 (M)