1QDD

CRYSTAL STRUCTURE OF HUMAN LITHOSTATHINE TO 1.3 A RESOLUTION

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]	298
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	P 65
Unit cell lengths	48.000, 48.000, 111.000
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 1.300
R-factor	0.132
R-free	0.15900
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	1.300	1.300
Rmerge	0.084	0.280
Total number of observations	114712 *
Number of reflections	32253
Completeness [%]	95.4	96.2
Redundancy		2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4	20 *	Pignol, D., (1995) Proteins: Struct.,Funct., Genet., 23, 604. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium acetate	100 (mM)	pH4.0
2	1	reservoir	PEG4000	12 (%(w/v))
3	1	drop	protein	7 (mg/ml)
4	1	drop	sodium acetate	50 (mM)
5	1	drop	PEG4000	6 (%(w/v))