1IWH

Crystal Structure of Horse Carbonmonoxyhemoglobin-Bezafibrate Complex at 1.55A Resolution: A Novel Allosteric Binding Site in R-State Hemoglobin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Temperature [K]	100
Detector technology	CCD
Collection date	2002-01-01
Detector	MAR CCD 165 mm
Wavelength(s)	1.0
Spacegroup name	C 2 2 21
Unit cell lengths	62.396, 107.496, 86.745
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.550
R-factor	0.174 *
R-free	0.23300 *
RMSD bond length	0.008
RMSD bond angle	0.082
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.610
High resolution limit [Å]	1.550	1.550
Rmerge	0.056	0.227
Total number of observations	186283 *
Number of reflections	40777
<I/σ(I)>	7.1
Completeness [%]	95.9	72.3
Redundancy	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Batch method *	6.8	20 *	PEG1000, pH 6.8, SMALL TUBES, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	hemoglobin solution	0.25 (%(w/v))
2	1	1	PEG1000	16 (%(w/v))
3	1	1	BZF	8 (mM)
4	1	1	sodium dithionite	0.1 (%(w/v))
5	1	1	citrate-ammonium	50 (mM)	pH6.8
6	1	1	glycerol	20 (%(v/v))