1H1O

Acidithiobacillus ferrooxidans cytochrome c4 structure supports a complex-induced tuning of electron transfer

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Collection date	2000-05-15
Spacegroup name	P 64 2 2
Unit cell lengths	100.049, 100.049, 149.668
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	35.000 * - 2.200 *
R-factor	0.239
Rwork	0.239
R-free	0.28400
Structure solution method	MAD
RMSD bond length	0.009
RMSD bond angle	19.700 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SOLVE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000 *	2.200
High resolution limit [Å]	2.200 *	2.130
Rmerge	0.041 *	0.245 *
Total number of observations	112983 *
Number of reflections	23012 *
<I/σ(I)>	8.2	2.3
Completeness [%]	99.7	99.7
Redundancy	4.9	5.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	2.9 *		MES 0.1M PH 6.5, PEG MME 30%, 10MM ZINC SULFATE, 5% GLYCEROL
1	Vapor diffusion *	2.9 *		MES 0.1M PH 6.5, PEG MME 30%, 10MM ZINC SULFATE, 5% GLYCEROL

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	glycine-HCl	20 (mM)	pH2.9
3	1	drop	ascorbate	1 (mM)
4	1	reservoir	MES	0.1 (M)	pH6.5
5	1	reservoir	PEG MME	25-30 (%)
6	1	reservoir	zinc sulfate	10 (mM)
7	1	reservoir	ascorbate	1 (mM)
8	1	reservoir	glycerol	5 (%)