1CEV

ARGINASE FROM BACILLUS CALDOVELOX, NATIVE STRUCTURE AT PH 5.6

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	113
Detector technology	IMAGE PLATE
Collection date	1996-11
Detector	RIGAKU
Spacegroup name	P 21 21 21
Unit cell lengths	83.600, 145.600, 155.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 2.400
R-factor	0.205 *
Rwork	0.205
R-free	0.26500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	LOW RESOLUTION STRUCTURE OF A DIFFERENT CRYSTAL FORM
RMSD bond length	0.012
RMSD bond angle	1.500
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]	40.000	2.600
High resolution limit [Å]	2.400	2.400
Rmerge	0.071	0.344
Total number of observations	286814 *
Number of reflections	68531
<I/σ(I)>	15.8	2.8
Completeness [%]	90.9	67.1
Redundancy	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6		3-6% N-BUTANOL,IN 0.1 M SODIUM CITRATE BUFFER, PH 5.6 PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS, PH 7.5, VAPOR DIFFUSION, HANGING DROP

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	27.3 (mg/ml)
2	1	drop	MOPS	10 (mM)
3	1	reservoir	n-butanol	3-6 (%)
4	1	reservoir	citrate	0.1 (M)