1E3C

Crystal structure of an Arylsulfatase A mutant C69S soaked in synthetic substrate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1998-08-15
Detector	MARRESEARCH
Spacegroup name	I 4 2 2
Unit cell lengths	131.800, 131.800, 192.100
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 2.650
R-factor	0.174
Rwork	0.173
R-free	0.24300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1auk
RMSD bond length	0.019
RMSD bond angle	0.053
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.750
High resolution limit [Å]	2.650	2.650
Rmerge	0.077 *	0.364 *
Number of reflections	24966
<I/σ(I)>	16.6	2.6
Completeness [%]	99.8	100
Redundancy	4.6	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4 *	18-22 *	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

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	10 (mM)
2	1	drop		150 (mM)
3	1	reservoir	sodium acetate	100 (mM)
4	1	reservoir	PEG6000	11-13 (%(w/v))