1KFR

Structural plasticity in the eight-helix fold of a trematode hemoglobin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X31
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-06-28
Detector	MARRESEARCH
Wavelength(s)	1.000
Spacegroup name	P 1 21 1
Unit cell lengths	41.117, 31.450, 54.952
Unit cell angles	90.00, 95.50, 90.00

Refinement procedure

Resolution	19.000 - 1.850
R-factor	0.161 *
Rwork	0.161
R-free	0.22000 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.120 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.000 *	1.880
High resolution limit [Å]	1.850	1.850
Rmerge	0.106 *
Total number of observations	66405 *
Number of reflections	12210
Completeness [%]	95.9	94.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	5.5	277	ammonium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	40 (mg/ml)
2	1	reservoir	ammonium sulfate	3.0 (M)
3	1	reservoir	sodium acetate	50 (mM)	pH5.5