1M56

Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	1998-12-12
Detector	ADSC QUANTUM 4
Wavelength(s)	1.0
Spacegroup name	H 3
Unit cell lengths	340.360, 340.360, 89.668
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.000 - 2.300
R-factor	0.236
Rwork	0.236
R-free	0.27500
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	0.040
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.400
High resolution limit [Å]	2.300	2.300
Rmerge	0.079 *	0.790 *
Total number of observations	232383 *
Number of reflections	119260 *	7880 *
Completeness [%]	69.3	36

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	4 *	PEG400, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	10 (mM)	pH8.0
10	1	reservoir		20 (mM)
11	1	reservoir	dodecylmaltoside	0.014 (%)
2	1	drop	decyl maltoside	0.24 (%)
3	1	drop	protein	10-20 (mg/ml)
4	1	reservoir	PEG400	18-22 (%)
5	1	reservoir		50-150 (mM)
6	1	reservoir	sodium citrate	100 (mM)	pH6.0
7	1	reservoir	Tris	10 (mM)
8	1	reservoir	decylmaltoside	0.24 (%)
9	1	reservoir	heptanetriol	2.5-3 (%)