4F0L

Crystal structure of Amidohydrolase from Brucella melitensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-12-18
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9774
Spacegroup name	P 1
Unit cell lengths	53.592, 62.192, 68.926
Unit cell angles	92.75, 95.49, 112.32

Refinement procedure

Resolution	50.000 - 2.050
R-factor	0.15
Rwork	0.148
R-free	0.18400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3mdu
RMSD bond length	0.013
RMSD bond angle	1.418
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.090
High resolution limit [Å]	2.050	5.560	2.050
Rmerge	0.086	0.064	0.211
Number of reflections	49766
<I/σ(I)>	8.4		3.8
Completeness [%]	97.9	99.1	96.5
Redundancy	2.2	2.2	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	290	Internal tracking number 226312A8 (JCSG A8). Crystallant: 20% PEG3350, 200 mM ammonium formate. Protein: BrabA.17379.a.A1 PS01212 at 36.85 mg/ml in a buffer consisting of 25 mM Hepes pH 7.0, 500 mM NaCl, 2 mM DTT, 0.025% sodium azide, and 5% glycerol., VAPOR DIFFUSION, SITTING DROP, temperature 290K