5CI5

Crystal Structure of an ABC transporter Solute Binding Protein from Thermotoga Lettingae TMO (Tlet_1705, TARGET EFI-510544) bound with alpha-D-Tagatose

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	2015-06-26
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	P 21 21 21
Unit cell lengths	73.363, 93.077, 103.637
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.619 - 1.610
R-factor	0.1337
Rwork	0.132
R-free	0.16790
Structure solution method	SAD
RMSD bond length	0.010
RMSD bond angle	1.290
Data reduction software	HKL-3000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.640
High resolution limit [Å]	1.610	4.370	1.610
Rmerge	0.113	0.052	0.957
Rmeas	0.117	0.054	0.992
Rpim	0.030	0.014	0.261
Total number of observations	1362797
Number of reflections	92888
<I/σ(I)>	6.2
Completeness [%]	100.0	99.3	100
Redundancy	14.7	14.2	14.2
CC(1/2)		0.997	0.895

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	298	Protein (10mM D-tagatose, 10 mM HEPES pH 7.5, 5 mM DTT); Reservoir (0.2 M Sodium chloride, 0.1M Bis-Tris HCl, 25%(w/v) PEG 3350); Cryoprotection (20% Diethylene glycol, 80% Reservoir)