1QFO

N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH 3'SIALYLLACTOSE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-6A
Synchrotron site	Photon Factory
Beamline	BL-6A
Temperature [K]	288
Detector technology	IMAGE PLATE
Detector	FUJI
Spacegroup name	P 21 21 21
Unit cell lengths	40.930, 97.590, 101.770
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.850
Rwork	0.200
R-free	0.23400
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	25.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.970
High resolution limit [Å]	1.850	1.850
Rmerge	0.071
Number of reflections	33750
Completeness [%]	94.6	84.2 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5.6	17 *	30 % (W/V) PEG 4000, 10 MM DTT, 0.1M SODIUM HEPES PH 5.6, 5MG/ML PROTEIN, 12.5MM 3'SIALYLLACTOSE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	3' sialyllactose	25 (mM)
3	1	reservoir	PEG4000	30 (%(w/v))
4	1	reservoir	sodium citrate	0.1 (M)
5	1	reservoir	ammonium acetate	0.2 (M)
6	1	reservoir	dithiothreitol	10 (mM)