2CEV

ARGINASE FROM BACILLUS CALDEVELOX, NATIVE STRUCTURE AT PH 8.5

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	113
Detector technology	IMAGE PLATE
Collection date	1996-12-15
Detector	RIGAKU
Spacegroup name	C 2 2 21
Unit cell lengths	106.220, 275.580, 138.070
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 2.150
R-factor	0.195 *
Rwork	0.195
R-free	0.23800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	LOW RESOLUTION STRUCTURE OF A DIFFERENT CRYSTAL FORM
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]	40.000	2.300
High resolution limit [Å]	2.150	2.150
Rmerge	0.067	0.271
Total number of observations	436708 *
Number of reflections	93307
<I/σ(I)>	15.4	3.1
Completeness [%]	87.9	63.2
Redundancy	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5		HANGING DROP VAPOUR DIFFUSION, MIXING 2 UL PROTEIN WITH 2 UL RESERVOIR SOLUTION. PROTEIN SOLUTION 27 MG/ML PROTEIN, 10 MM MOPS,PH 7.5. RESERVOIR SOLUTION 27-30% MONOMETHYLPEG 5000, 10 MM MNCL2, 10 MM GUANIDINE HYDROCHLORIDE, IN 0.1 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	drop	protein	27.3 (mg/ml)
2	1	drop	MOPS	10 (mM)
3	1	reservoir	mPEG5000	27-30 (%)
4	1	reservoir		10 (mM)
5	1	reservoir	guanidine hydrochloride	10 (mM)
6	1	reservoir	Bis-Tris propane/HCl	0.1 (M)