3UPD

2.9 Angstrom Crystal Structure of Ornithine Carbamoyltransferase (ArgF) from Vibrio vulnificus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2011-11-10
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97903
Spacegroup name	I 21 3
Unit cell lengths	153.963, 153.963, 153.963
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.110 - 2.910
R-factor	0.15978
Rwork	0.158
R-free	0.19452
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1duv
RMSD bond length	0.011
RMSD bond angle	1.488
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.950
High resolution limit [Å]	2.900	2.900
Rmerge	0.095	0.597
Number of reflections	13533
<I/σ(I)>	18.3	3.3
Completeness [%]	100.0	100
Redundancy	6	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	295	Protein: 7.2mG/mL, 0.25M Sodium chloride, 0.01M Tris-HCl (pH 8.3); Screen: Calssics II (C2), 1.1M Ammonium tartrate (pH 7.0); Cryo: 4.0M Sodium formate, VAPOR DIFFUSION, SITTING DROP, temperature 295K