3I09

CRYSTAL STRUCTURE OF A PERIPLASMIC BINDING PROTEIN (BMA2936) FROM BURKHOLDERIA MALLEI AT 1.80 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	2009-03-19
Detector	MARMOSAIC 325 mm CCD
Wavelength(s)	0.91162,0.97925,0.97903
Spacegroup name	P 1 21 1
Unit cell lengths	58.255, 81.151, 73.996
Unit cell angles	90.00, 92.86, 90.00

Refinement procedure

Resolution	29.709 - 1.800
R-factor	0.139
Rwork	0.137
R-free	0.17400
Structure solution method	MAD
RMSD bond length	0.016
RMSD bond angle	1.459
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHELX
Refinement software	REFMAC (5.5.0053)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.709	29.709	1.860
High resolution limit [Å]	1.800	3.870	1.800
Rmerge	0.051	0.023	0.324
Number of reflections	63635	12214	11335
<I/σ(I)>	11.41	28.9	2.7
Completeness [%]	98.1	96.4	95.9
Redundancy	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4	277	20.0000% PEG-6000, 0.1M Citrate pH 4.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K