4CEV

ARGINASE FROM BACILLUS CALDEVELOX, L-ORNITHINE 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	106.600, 277.300, 139.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.700
R-factor	0.203 *
Rwork	0.203
R-free	0.27400
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	2.900
High resolution limit [Å]	2.700	2.700
Rmerge	0.097	0.219
Total number of observations	161259 *
Number of reflections	53853
<I/σ(I)>	10.1	3
Completeness [%]	93.5	82.4
Redundancy	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5		RESERVOIR SOLUTION 28% MONOMETHYLPEG 2000, 5 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, 10 MM D/L-ORNITHINE,IN 0.05 M BISTRISPROPANE/HCL,PH 8.5 27 MG/ML PROTEIN, 10 MM MOPSm, PH 7.5 , 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	D/L-ornithine	10 (mM)