5IBQ

Crystal structure of an ABC solute binding protein from Rhizobium etli CFN 42 (RHE_PF00037,TARGET EFI-511357) in complex with alpha-D-apiose

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	2015-12-11
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	C 1 2 1
Unit cell lengths	93.272, 36.924, 95.619
Unit cell angles	90.00, 118.02, 90.00

Refinement procedure

Resolution	30.979 - 1.200
R-factor	0.1506
Rwork	0.150
R-free	0.16400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ry0
RMSD bond length	0.007
RMSD bond angle	0.969
Data reduction software	MOSFLM
Data scaling software	Aimless (0.2.8)
Refinement software	PHENIX (1.10.1_2155)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	41.170	41.170	1.220
High resolution limit [Å]	1.200	6.460	1.200
Rmerge	0.068	0.025	0.674
Rmeas	0.079	0.030	0.789
Rpim	0.041	0.016	0.408
Total number of observations	319876	1936	15425
Number of reflections	85430
<I/σ(I)>	11.7	36.5	2
Completeness [%]	95.1	91.4	92
Redundancy	3.7	3.4	3.7
CC(1/2)	0.999	0.998	0.726

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	298	Protein (10 mM HEPES pH 7.5, 5 mM DTT, 10 mM D-apiose) incubate at 37 degrees C for 30 minutes; Reservoir (MCSG1 B6, 0.2 M Calcium Acetate, 0.1 M MES pH 6.0, 20 %(w/v) PEG 8000); Cryoprotection (20% glucose)