3SJT

Crystal structure of human arginase I in complex with the inhibitor Me-ABH, Resolution 1.60 A, twinned structure

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2008-02-03
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.0
Spacegroup name	P 3
Unit cell lengths	90.337, 90.337, 69.329
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	34.068 - 1.597
R-factor	0.1301
Rwork	0.129
R-free	0.16310
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2zav
RMSD bond length	0.006
RMSD bond angle	1.040
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.700
High resolution limit [Å]	1.597	1.597
Rmerge	0.050	0.298
Number of reflections	82598
<I/σ(I)>	25.1	2.7
Completeness [%]		95.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.8	298	3 uL of protein solution [3.5 mg/mL HAI, 50 mM bicine (pH 8.5), 2 mM MABH, 100 M MnCl2] and 3 uL of precipitant solution [0.1 M HEPES (pH 7.0), 22-28% Jeffamine] were equilibrated against a 1 mL reservoir of precipitant solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K