1HQ5

CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH S-(2-BORONOETHYL)-L-CYSTEINE, AN L-ARGININE ANALOGUE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-10-13
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 3
Unit cell lengths	91.300, 91.300, 69.400
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.300
Rwork	0.158
R-free	0.19400
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.007
RMSD bond angle	23.300 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.098	0.242
Total number of observations	41944 *
Number of reflections	14462 *
<I/σ(I)>	8
Completeness [%]	98.1 *	97.5
Redundancy	2.9	2.85

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	4 *	drop consists of equal amounts of protein and precipitant solutions *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	BEC	3 (mM)
3	1	drop		5 (mM)
4	1	drop	bicine-NaOH	25 (mM)
5	1	reservoir	PEG1500	24 (%)	precipitant
6	1	reservoir	bicine-NaOH	100 (mM)	precipitant