1APY

HUMAN ASPARTYLGLUCOSAMINIDASE

Experimental procedure

Source type	ROTATING ANODE
Detector technology	IMAGE PLATE
Collection date	1994-12-10
Detector	RIGAKU
Spacegroup name	P 61
Unit cell lengths	98.400, 98.400, 134.500
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.000
R-factor	0.169
Rwork	0.169
R-free	0.22400
RMSD bond length	0.007
RMSD bond angle	1.400
Data reduction software	HKL
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000 *
High resolution limit [Å]	2.000 *	2.000 *
Rmerge	0.065
Total number of observations	95095 *
Number of reflections	37768 *
Completeness [%]	76.2 *	34.2 *
Redundancy	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.9 *	20 *	Tikkanen, R., (1996) Protein Struct. Func. Genet., 24, 253. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	10 (mg/ml)
2	1	reservoir	PEG4000	18 (%(w/v))
3	1	reservoir	acetate	20 (mM)
4	1	reservoir		1 (mM)