1E2S

Crystal structure of an Arylsulfatase A mutant C69A

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	1999-02-15
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 - 2.350
R-factor	0.194
Rwork	0.191
R-free	0.23600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1auk
RMSD bond length	0.014
RMSD bond angle	0.045
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.450
High resolution limit [Å]	2.350	2.350
Number of reflections	35243
<I/σ(I)>	16.9	2.8
Completeness [%]	99.3	100
Redundancy	4.5	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.4	291	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