3E8Z

X-ray structure of rat arginase I-N130A mutant: the unliganded complex

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
Wavelength(s)	1.0
Spacegroup name	P 32
Unit cell lengths	87.500, 87.500, 100.110
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	41.770 - 2.000
R-factor	0.236
Rwork	0.236
R-free	0.28000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rla
RMSD bond length	0.006
RMSD bond angle	1.300
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	CNS (1.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	60.400	2.100
High resolution limit [Å]	2.000	2.000
Rmerge	0.077	0.260
Number of reflections	53201
<I/σ(I)>	12.3	3
Completeness [%]	91.8	66.1
Redundancy	2.9	1.9

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 3350, 0.2 M NaCl] were equilibrated over a 1 mL reservoir of precipitant solution., VAPOR DIFFUSION, HANGING DROP