2Q04

Crystal structure of acetoin utilization protein (ZP_00540088.1) from Exiguobacterium sibiricum 255-15 at 2.33 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-2
Synchrotron site	SSRL
Beamline	BL9-2
Temperature [K]	100
Detector technology	CCD
Collection date	2007-03-15
Detector	MARMOSAIC 325 mm CCD
Wavelength(s)	0.91162, 0.97936, 0.97925
Spacegroup name	P 1 21 1
Unit cell lengths	70.870, 128.580, 108.430
Unit cell angles	90.00, 108.43, 90.00

Refinement procedure

Resolution	29.336 - 2.330
R-factor	0.231
Rwork	0.229
R-free	0.26000
Structure solution method	MAD
RMSD bond length	0.014
RMSD bond angle	0.756
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHELX
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.336		2.410
High resolution limit [Å]	2.330	5.000	2.330
Rmerge	0.052	0.021	0.450
Number of reflections	73748	13438	13452
<I/σ(I)>	7.53	20	1.4
Completeness [%]	88.6	85.1	89.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	277	NANODROP, 5.7% PEG 8000, 0.2M Calcium acetate, 0.1M Imidazole pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K