6UPD

Structure of trehalose-6-phosphate phosphatase from Salmonella typhimurium in complex with trehalose

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	290
Detector technology	PIXEL
Collection date	2017-11-14
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97919
Spacegroup name	P 1 21 1
Unit cell lengths	46.767, 52.955, 108.762
Unit cell angles	90.00, 100.61, 90.00

Refinement procedure

Resolution	53.451 - 2.052
R-factor	0.221
Rwork	0.218
R-free	0.26150
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6upb
Data reduction software	XDS
Data scaling software	Aimless (0.5.23)
Phasing software	PHASER (2.8.1)
Refinement software	PHENIX (1.13_2998)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	106.900	106.900	2.110
High resolution limit [Å]	2.050	8.950	2.050
Rmerge	0.084	0.039	0.859
Rmeas	0.098	0.046	1.007
Rpim	0.051	0.025	0.519
Total number of observations	117234	1452	8098
Number of reflections	32534	433	2270
<I/σ(I)>	9.4	28.8	1.2
Completeness [%]	98.6	99.6	88.8
Redundancy	3.6	3.4	3.6
CC(1/2)	0.997	0.997	0.577

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		290	Drop Contained: 2 uL 40 mg/mL protein, 2 uL reservoir solution (16% PEG 3350, 450 mM lithium citrate and 10 mM magnesium chloride) and 0.5 uL 1:10^3 dilution of seed stock prepared according to the Seed Bead protocol. Crystals were transferred to a drop containing 35% PEG 3350, 166 mM lithium citrate, 166 mM magnesium chloride, 10% ethylene glycol and 50 mM trehalose for 30 minutes prior to cryocooling.