3E9B

X-ray structure of rat arginase I-T135A mutant: the complex with BEC

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F2
Synchrotron site	CHESS
Beamline	F2
Temperature [K]	100
Detector technology	CCD
Detector	ADSC QUANTUM 210
Spacegroup name	P 32
Unit cell lengths	87.505, 87.505, 100.696
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.150
R-factor	0.216
Rwork	0.216
R-free	0.27400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rla
RMSD bond length	0.006
RMSD bond angle	1.400
Refinement software	CNS (1.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.250
High resolution limit [Å]	2.150	2.150
Rmerge	0.107	0.356
Number of reflections	46355
<I/σ(I)>	10.2	2.1
Completeness [%]	98.8	91.2
Redundancy	3.1	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP			drops containing 3 microL of protein solution [5 mg/mL protein, 50 mM bicine (pH 8.5), 2 mM BEC, 2 mM MnCl2] and 3 microL of precipitant solution [0.1 M CHES (pH 9.5), 20% PEG 8000] were equilibrated over a 1 mL reservoir of precipitant solution. , VAPOR DIFFUSION, HANGING DROP