3D64

Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2008-04-02
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.03317
Spacegroup name	P 32 2 1
Unit cell lengths	186.363, 186.363, 104.403
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.300
R-factor	0.172
Rwork	0.171
R-free	0.20200
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.246
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.4.0067)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.380
High resolution limit [Å]	2.300	4.950	2.300
Rmerge	0.125	0.043	0.649
Number of reflections	92618
<I/σ(I)>	7.7
Completeness [%]	100.0	100	99.9
Redundancy	6.8	6.8	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.25	289	21.5 mg/ml Protein, 20% PEG 3350, 200mM Na acetate, 5% Glycerol, 25mM Hepes, 500mM NaCl, 0.025M Na Azide, pH 7.25, VAPOR DIFFUSION, SITTING DROP, temperature 289K