3MFW

Crystal structure of human arginase I in complex with L-2-aminohistidine and sulphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X6A
Synchrotron site	NSLS
Beamline	X6A
Detector technology	CCD
Collection date	2008-12-01
Detector	ADSC QUANTUM 210
Wavelength(s)	1.0
Spacegroup name	P 3
Unit cell lengths	90.338, 90.338, 69.429
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 1.470
R-factor	0.149
Rwork	0.149
R-free	0.16200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2zav
RMSD bond length	0.011
RMSD bond angle	2.200
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.560
High resolution limit [Å]	1.470	1.470
Rmerge	0.059	0.616
Number of reflections	107754
<I/σ(I)>	21.1	2.3
Completeness [%]	99.4	99.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		298	Crystals of HAI-2AH-SO4 complex were prepared by soaking 2AH into pre-formed crystals of the native enzyme, which were prepared by the hanging drop vapor diffusion method at 21 C. Drops containing 3 uL of protein solution [3.5 mg/mL protein, 50.0 mM bicine (pH 8.5), 2 mM thymine, 100 M MnCl2] and 3 uL of precipitant solution [0.1 M HEPES (pH 7.0), 28% Jeffamine] were equilibrated against a 1 mL reservoir of precipitant buffer., VAPOR DIFFUSION, HANGING DROP, temperature 298K