6WCX

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Synchrotron site	Australian Synchrotron
Beamline	MX1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-03-20
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.954
Spacegroup name	P 61 2 2
Unit cell lengths	86.957, 86.957, 454.712
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.190 - 2.890
R-factor	0.2271
Rwork	0.225
R-free	0.26060
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 (1.18rc1-3769)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	49.190	49.190	3.070
High resolution limit [Å]	2.890	8.680	2.890
Rmerge	0.223	0.107	1.137
Rmeas	0.235	0.112	1.213
Rpim	0.069	0.029	0.380
Total number of observations		15977	26252
Number of reflections	23922	1082	3641
<I/σ(I)>	7.7	26.8	1.6
Completeness [%]	99.4	99.5	97.4
Redundancy	9.1	14.8	7.2
CC(1/2)	0.988	0.995	0.524

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289.15	0.4 uL ~8.0 mg/mL FphF (10 mM HEPES pH 7.5, 10 mM NaCl) were mixed with 0.07 uL ligand solution (~0.5 mM 4-Methylumbelliferyl heptanoate in 100% DMSO) and 0.4 uL of reservoir solution. Sitting drop reservoir contained 50 uL of 0.8 M Sodium formate, 0.1 M Tris pH 7.5, 10 % w/v PEG 8000 and 10 % w/v PEG 1000. Crystals were soaked for ~15 seconds in 75% reservoir solution and 25% glycerol prior to freezing in liquid nitrogen