2OLP

Structure and ligand selection of hemoglobin II from Lucina pectinata

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM16
Synchrotron site	ESRF
Beamline	BM16
Temperature [K]	100
Detector technology	CCD
Collection date	2004-07-01
Detector	MAR CCD 165 mm
Wavelength(s)	0.97749
Spacegroup name	P 42 21 2
Unit cell lengths	73.918, 73.918, 152.355
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.838 - 1.932
Rwork	0.165
R-free	0.19320
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ebt
RMSD bond length	0.013
RMSD bond angle	1.841
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	REFMAC (refmac_5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.960
High resolution limit [Å]	1.930	1.930
Rmerge	0.050	0.336
Number of reflections	32364
<I/σ(I)>	28.81	7
Completeness [%]	99.6	100
Redundancy	10.5	10.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	COUNTER-DIFFUSION	7	298	Reactor: 0.2 mm inner diameter capillary with a three layer configuration (6 microL/ 3 microL/ 30 microL). Protein chamber: 30 mg/ml in 50 mM BIS-TRIS propane pH 7.0, 0.5 mM EDTA, agarose 0.08% (w/v). Precipitant chamber: Ammonium sulphate 2.0 M., Counter-diffusion, temperature 298K