1AUK

HUMAN ARYLSULFATASE A

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1996-03
Detector	MARRESEARCH
Spacegroup name	I 4 2 2
Unit cell lengths	132.630, 132.630, 192.060
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.100
R-factor	0.248
Rwork	0.232
R-free	0.27300
Structure solution method	MIRAS
RMSD bond length	0.013
RMSD bond angle	1.800
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.200
High resolution limit [Å]	2.100	2.100
Rmerge	0.063 *	0.276 *
Number of reflections	49794
<I/σ(I)>	9.4	4.3
Completeness [%]	96.1	96.7 *
Redundancy	6.2	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.4	18 *	PROTEIN WAS CRYSTALLIZED BY VAPOR DIFFUSION IN HANGING DROPS AT 291 K. SOLUTION CONTAINING 10MG/ML PROTEIN, 10 MM TRIS/HCL (PH 7.4) AND 150 MM NACL WAS MIXED WITH SAME VOLUME OF RESERVOIR SOLUTION, CONTAINING 100 MM NA-ACETATE (PH 5.0 - 5.4) AND 10 - 13 % PEG 6000, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium acetate	100 (mM)
2	1	reservoir	PEG6000	10-13 (%)
3	1	drop	sodium acetate	100 (mM)
4	1	drop	PEG6000	10-13 (%)
5	1	drop	octyl-beta-glucopyranoside	1.25 (%)
6	1	drop	Tris-HCl	10 (mM)
7	1	drop		150 (mM)