6VH9

FphF, Staphylococcus aureus fluorophosphonate-binding serine hydrolases F, apo form

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	87.145, 87.145, 453.600
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	43.570 - 1.710
R-factor	0.1777
Rwork	0.176
R-free	0.20080
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4rgy
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]	49.160	49.160	1.740
High resolution limit [Å]	1.710	9.350	1.710
Rmerge	0.128	0.041	3.155
Rmeas	0.130	0.042	3.215
Rpim	0.025	0.009	0.605
Total number of observations		17638	144842
Number of reflections	112281	900	5332
<I/σ(I)>	16.5	55.2	1.5
Completeness [%]	99.9	99.5	97.8
Redundancy	27.3	19.6	27.2
CC(1/2)	0.999	1.000	0.581

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289.15	0.2 uL ~8.5 mg/ml FphF (20 mM HEPES pH 7.5, 10 mM NaCl) were mixed with 0.1 uL FphF crystal seeds (in 54.4% Tacsimate pH 7.0, 0.1 M Bis-Tris propane pH 6.5, 8% Polypropylene glycol P 400) and 0.2 uL of reservoir solution. Sitting drop reservoir contained 50 uL of 2.8 M Sodium acetate. Crystals were soaked for ~20 seconds in 75% reservoir solution and 25% ethylenglycol prior to freezing in liquid nitrogen