1I0H

CRYSTAL STRUCTURE OF THE E. COLI MANGANESE SUPEROXIDE DISMUTASE MUTANT Y174F AT 1.35 ANGSTROMS RESOLUTION.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	110
Detector technology	AREA DETECTOR
Collection date	1998-11-01
Detector	MARRESEARCH
Wavelength(s)	0.9058
Spacegroup name	P 1 21 1
Unit cell lengths	46.893, 46.017, 95.993
Unit cell angles	90.00, 98.40, 90.00

Refinement procedure

Resolution	50.000 - 1.350
R-factor	0.169
Rwork	0.170
R-free	0.19600
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.015
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.370
High resolution limit [Å]	1.350	1.350
Rmerge	0.027	0.071
Total number of observations	561459 *
Number of reflections	89109
<I/σ(I)>	52.5	18.3
Completeness [%]	100.0	99.9
Redundancy	4.2	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	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)