1AYY

GLYCOSYLASPARAGINASE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	130
Detector technology	IMAGE PLATE
Collection date	1996-11
Detector	RIGAKU
Spacegroup name	P 1 21 1
Unit cell lengths	46.200, 115.600, 52.400
Unit cell angles	90.00, 107.20, 90.00

Refinement procedure

Resolution	20.000 - 2.320
R-factor	0.188
Rwork	0.188
R-free	0.27000
Structure solution method	MOLECULAR REPLACEMENT + PHASE COMBINATION WITH 2 DERIVATIVES
Starting model (for MR)	HUMAN GLYCOSYLASPARAGINASE DIMER
RMSD bond length	0.003
RMSD bond angle	25.280 *
Data reduction software	bioteX
Data scaling software	bioteX
Phasing software	AMoRE
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.400
High resolution limit [Å]	2.320	2.320
Rmerge	0.075	0.170
Number of reflections	22627
<I/σ(I)>	7	3
Completeness [%]	95.7	72.2
Redundancy	2.9	2.73

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	10 *	19% PEG3350 IN 100 MM TRIS.HCL PH 8.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.8 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)
3	1	drop		5 (mM)
4	1	drop	EDTA	1 (mM)
5	1	reservoir	PEG3350	19 (%)
6	1	reservoir	Tris-HCl	100 (mM)