1R46

Structure of human alpha-galactosidase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2003-02-23
Detector	MARRESEARCH
Wavelength(s)	1.033
Spacegroup name	P 32 2 1
Unit cell lengths	88.458, 88.458, 215.482
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 * - 3.250
R-factor	0.262
Rwork	0.262
R-free	0.30100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Homology model derived from 1KTB
RMSD bond length	0.009
RMSD bond angle	22.800 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000 *	3.370
High resolution limit [Å]	3.250	3.250
Rmerge	0.246	0.740
Total number of observations	156309 *
Number of reflections	16080 *	1542 *
<I/σ(I)>	9.7	2.4
Completeness [%]	99.8 *	98.7
Redundancy	9.7	6.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	293	30% PEG 4000, 0.1M TRIS HCL (PH 8.0), 0.2M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	40 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)	pH7.5
3	1	reservoir	PEG4000	30 (%(w/v))
4	1	reservoir	Tris-HCl	100 (mM)	pH8.0
5	1	reservoir	ammonium sulfate	200 (mM)