1HLQ

CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
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	1997-04-23
Detector	MARRESEARCH
Wavelength(s)	1.105
Spacegroup name	P 43 21 2
Unit cell lengths	88.312, 88.312, 61.340
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	22.000 - 1.450
R-factor	0.186
Rwork	0.187
R-free	0.21800
Structure solution method	MAD
RMSD bond length	0.008
RMSD bond angle	8.400 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SHARP
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	22.090	1.530
High resolution limit [Å]	1.450	1.450
Rmerge	0.047	0.412
Total number of observations	239390 *
Number of reflections	42770 *	41858 *
<I/σ(I)>	6.9	0.6
Completeness [%]	99.0	95.4
Redundancy	5.6	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8	293 *	HiPIP (20mg/ml, 20mM Tris pH 8, 2mM Beta-mercaptoethanol, 3.2M (NH4)2SO4 in 100mM Tris buffer, VAPOR DIFFUSION, HANGING DROP, temperature 290K
1	Vapor diffusion *	8	293 *	HiPIP (20mg/ml, 20mM Tris pH 8, 2mM Beta-mercaptoethanol, 3.2M (NH4)2SO4 in 100mM Tris buffer, VAPOR DIFFUSION, HANGING DROP, temperature 290K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)	pH8.
3	1	drop	beta-mercaptoethanol	2 (mM)
4	1	reservoir	ammonium sulfate	3.2 (M)
5	1	reservoir	Tris-HCl	100 (mM)	pH8.