5IJG

Crystal structure of O-acetylhomoserine sulfhydrolase from Brucella melitensis at 2.0 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL41XU
Synchrotron site	SPring-8
Beamline	BL41XU
Temperature [K]	100
Detector technology	PIXEL
Collection date	2012-06-14
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	1.0
Spacegroup name	P 32 2 1
Unit cell lengths	109.710, 109.710, 110.770
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	95.010 - 2.000
R-factor	0.17246
Rwork	0.170
R-free	0.22346
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3NMY
RMSD bond length	0.019
RMSD bond angle	1.951
Data reduction software	iMOSFLM
Data scaling software	Aimless (0.5.17)
Phasing software	BALBES
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	95.010	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.104	1.164
Rmeas	0.107
Rpim	0.025
Total number of observations	960069
Number of reflections	52389
<I/σ(I)>	19.6
Completeness [%]	99.9	99.5
Redundancy	18.3	16
CC(1/2)	0.999

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	100 mM di-ammonium tartrate pH 7.0, 12% PEG3350, 4 mM n-decyl-b-D-maltopyranoside