1QO8

The structure of the open conformation of a flavocytochrome c3 fumarate reductase

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-04-15
Detector	MARRESEARCH
Wavelength(s)	0.8469, 1.033, 1.739, 1.741
Spacegroup name	P 21 21 21
Unit cell lengths	71.770, 109.690, 227.320
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.150
R-factor	0.225 *
Rwork	0.225
R-free	0.28100
Structure solution method	MAD
RMSD bond length	0.015
RMSD bond angle	0.013
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.190
High resolution limit [Å]	2.150	2.150
Rmerge	0.038 *	0.274 *
Total number of observations	1428311 *
Number of reflections	97968
Completeness [%]	93.4 *	91.4
Redundancy	14.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *		Bamford, V., (1999) Acta Crystallogr.,Sect., D55, 1222. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-15 (mg/ml)
2	1	drop	sodium HEPES	50 (mM)
3	1	drop		100 (mM)
4	1	reservoir	PEG10000	6-15 (%(w/v))
5	1	reservoir	sodium MES