5CEV

ARGINASE FROM BACILLUS CALDEVELOX, L-LYSINE COMPLEX

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	113
Detector technology	IMAGE PLATE
Collection date	1997-01
Detector	RIGAKU
Spacegroup name	C 2 2 21
Unit cell lengths	106.400, 277.000, 138.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.500
R-factor	0.212 *
Rwork	0.212
R-free	0.26100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	REFINED MODEL FOR THE PH 8.5 NATIVE STRUCTURE: 2CEV
RMSD bond length	0.011
RMSD bond angle	1.470
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.700
High resolution limit [Å]	2.500	2.500
Rmerge	0.067	0.188
Total number of observations	424670 *
Number of reflections	68127
<I/σ(I)>	18	4.8
Completeness [%]	94.9	72.7
Redundancy	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5		MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS, PH 7.5 RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 5 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM L-LYSINE, IN 0.05 M BISTRISPROPANE/HCL, PH 8.5 , VAPOR DIFFUSION, HANGING DROP

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	mmPEG2000	28 (%)
2	1	reservoir	guanidine hydrochloride	10 (mM)
3	1	reservoir		5 (mM)
4	1	reservoir	BTP/HCl	50 (mM)
5	1	reservoir	L-lysine	10 (mM)