6VHD

FphF, Staphylococcus aureus fluorophosphonate-binding serine hydrolases F, KT129 bound

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-07-31
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.954
Spacegroup name	P 61 2 2
Unit cell lengths	87.202, 87.202, 455.197
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.280 - 1.980
R-factor	0.178
Rwork	0.176
R-free	0.21310
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6vh9
Data reduction software	XDS
Data scaling software	Aimless (0.7.4)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (dev-3699)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	49.280	49.280	2.020
High resolution limit [Å]	1.980	9.700	1.980
Rmerge	0.151	0.037	2.676
Rmeas	0.154	0.038	2.730
Rpim	0.029	0.008	0.535
Total number of observations		16651	107296
Number of reflections	73040	809	4307
<I/σ(I)>	16.7	63.1	1.5
Completeness [%]	99.9	99.4	98.5
Redundancy	27.1	20.6	24.9
CC(1/2)	0.999	1.000	0.711

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289.15	0.2 uL ~7.5 mg/ml FphF+KT129 (0.12mM KT129, 12% DMSO, 18 mM HEPES pH 7.5, 8 mM NaCl) were mixed with 0.2 uL of reservoir solution. Sitting drop reservoir contained 50 uL of 0.2 M Sodium citrate, 0.1 M Bis-Tris propane pH 6.5, 20% w/v PEG 3350. Crystals were soaked for ~20 seconds in 75% reservoir solution and 25% glycerol prior to freezing in liquid nitrogen