4YLE

Crystal structure of an ABC transpoter solute binding protein (IPR025997) from Burkholderia multivorans (Bmul_1631, Target EFI-511115) with an unknown ligand modelled as alpha-D-erythrofuranose

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 31-ID
Synchrotron site	APS
Beamline	31-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2015-02-24
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	P 21 21 21
Unit cell lengths	32.966, 69.267, 115.060
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.437 - 1.700
R-factor	0.1731
Rwork	0.171
R-free	0.21090
Structure solution method	SAD
RMSD bond length	0.011
RMSD bond angle	1.343
Data scaling software	Aimless (0.5.1)
Refinement software	PHENIX ((phenix.refine: 1.9_1692))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.670	29.670	1.730
High resolution limit [Å]	1.700	9.000	1.700
Rmerge	0.100	0.075	0.816
Rpim	0.031	0.026	0.249
Total number of observations	309119	1625	15273
Number of reflections	28926
<I/σ(I)>	15.4	29.2	2.8
Completeness [%]	96.8	77.1	88.6
Redundancy	10.7	8.2	11
CC(1/2)	0.998	0.992	0.840

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	298	Protein (10 mM HEPES pH 7.5, 5 mM DTT); Reservoir (MCSG1 G7, 0.1 M Tris pH 8.5, 25% (w/v) PEG 3350); Cryoprotection (20% glycerol, 80% Reservoir)