3CEV

ARGINASE FROM BACILLUS CALDEVELOX, COMPLEXED WITH L-ARGININE

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	106.800, 277.700, 140.000
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.400
R-factor	0.193 *
Rwork	0.193
R-free	0.24300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	REFINED MODEL FOR THE PH 8.5 NATIVE STRUCTURE: 2CEV
RMSD bond length	0.010
RMSD bond angle	1.420
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 *	2.550
High resolution limit [Å]	2.400	2.400
Rmerge	0.052	0.169
Total number of observations	201956 *
Number of reflections	73511
<I/σ(I)>	14.1	3.8
Completeness [%]	89.7	52.4
Redundancy	2.75

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, 10 MM EDTA, 10 MM GUANIDINE HYDROCHLORIDE, IN 0.05 M BISTRISPROPANE/HCL, PH 8. THE CRYSTALS WERE THEN SOAKED IN 42.5% MMPEG 2000, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM L-ARGININE, 10 MM EDTA, 0.05M BISTRISPROPANE/HCL, PH 8.5 FOR 8 HOURS, 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	EDTA	10 (mM)
4	1	reservoir	BTP/HCl	50 (mM)