6UPC

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-1
Synchrotron site	NSLS-II
Beamline	17-ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-10-24
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.9201
Spacegroup name	P 1 21 1
Unit cell lengths	46.525, 52.639, 107.053
Unit cell angles	90.00, 99.23, 90.00

Refinement procedure

Resolution	29.273 - 2.505
R-factor	0.1969
Rwork	0.193
R-free	0.22770
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6upb
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.13_2998)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.273	2.595
High resolution limit [Å]	2.505	2.505
Rmerge	0.075	0.480
Number of reflections	17698	1678
<I/σ(I)>	8.03
Completeness [%]	99.2	94.69
Redundancy	2
CC(1/2)	0.993	0.616

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 (19% PEG 3350, 375 mM lithium citrate, 10 mM magnesium chloride 2% 1,4 dioxane) and 0.5 uL 1:10^9 dilution of seed stock prepared according to the Seed Bead protocol. Crystals were transferred to a drop containing 24% PEG 3350, 50 mM lithium citrate, 100 mM magnesium chloride, 10% ethylene glycol and 5 mM trehalose 6-phosphate for 1 hours prior to cryocooling