3WCT

The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: Oxygenated form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44XU
Synchrotron site	SPring-8
Beamline	BL44XU
Temperature [K]	100
Detector technology	CCD
Collection date	2009-07-06
Detector	Bruker DIP-6040
Wavelength(s)	0.9000
Spacegroup name	P 63
Unit cell lengths	108.556, 108.556, 193.552
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	43.020 - 2.400
R-factor	0.216
Rwork	0.216
R-free	0.26400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1yhu
RMSD bond length	0.007
RMSD bond angle	1.100
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	CNS (1.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.490
High resolution limit [Å]	2.400	2.400
Number of reflections	50516
<I/σ(I)>	28.6	6.7
Completeness [%]	100.0	100
Redundancy	11.7	11.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	13-18% PEG 3350, 0-5mM Ca acetate/Mg acetate, 100mM HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K