1I08

CRYSTAL STRUCTURE ANALYSIS OF THE H30A MUTANT OF MANGANESE SUPEROXIDE DISMUTASE FROM E. COLI

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1998-06-02
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	C 2 2 21
Unit cell lengths	100.681, 109.110, 181.072
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 2.200
R-factor	0.184
Rwork	0.184
R-free	0.21100
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	1.160
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.250
High resolution limit [Å]	2.200	2.200
Rmerge	0.059	0.260
Total number of observations	458707 *
Number of reflections	48514
<I/σ(I)>	22.4	4
Completeness [%]	95.3	73
Redundancy	5.3	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	298	drop consists of 2 micro litter of protein solution in 0.1 M bicine plus 2 micro litter of reservoir solution *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	18-20 (mg/ml)
2	1	drop	Bicine	0.1 (M)
3	1	reservoir	PEG6000	16-20 (%)
4	1	reservoir	bicine	0.1 (M)