1HMU

ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X8C
Synchrotron site	NSLS
Beamline	X8C
Temperature [K]	100
Detector technology	CCD
Collection date	1999-02-02
Detector	ADSC QUANTUM 4
Spacegroup name	P 43 21 2
Unit cell lengths	86.900, 86.900, 192.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
Rwork	0.227
R-free	0.26600
RMSD bond length	0.006
RMSD bond angle	1.340
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.000	2.000
Rmerge	0.063	0.302
Total number of observations	282695 *
Number of reflections	49755
<I/σ(I)>	14.3
Completeness [%]	98.6	98.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	PEG 3350, sodium acetate, hepes , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG3350	15 (%(w/v))
2	1	reservoir	sodium acetate	400 (mM)
3	1	reservoir	HEPES	100 (mM)