3GMZ

Crystal of human arginase in complex with L-ornithine. Resolution 1.43 A.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	CCD
Collection date	2008-06-13
Detector	ADSC QUANTUM 315
Wavelength(s)	1.0
Spacegroup name	P 3
Unit cell lengths	90.392, 90.392, 69.422
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 1.430
Rwork	0.147
R-free	0.18500
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	2zav
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.530
High resolution limit [Å]	1.430	1.430
Rmerge	0.067	0.640
Number of reflections	116771
<I/σ(I)>	35.6	2
Completeness [%]	99.8	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2	298	Crystalline DFMO and L-ornithine complexes with human arginase I were prepared by soaking these ligands into pre-formed crystals of the native enzyme, which were prepared by the hanging drop vapor diffusion method at 21 C. Typically, drops containing 3 uL of protein solution [3.5 mg/mL protein, 50 mM bicine (pH 8.5), 2 mM thymine, 100 uM MnCl2] and 3 uL of precipitant solution [0.1 M bis-Tris (pH 6.5), 28% PEG monomethyl ether 2000] were equilibrated over a 1 mL reservoir of precipitant solution. VAPOR DIFFUSION, HANGING DROP, temperature 298K