6VHE

FphF, Staphylococcus aureus fluorophosphonate-binding serine hydrolases F, KT130 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	2019-09-21
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.954
Spacegroup name	P 61 2 2
Unit cell lengths	87.126, 87.126, 454.920
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.240 - 1.940
R-factor	0.1701
Rwork	0.168
R-free	0.20860
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]	49.240	49.240	1.980
High resolution limit [Å]	1.940	9.690	1.940
Rmerge	0.152	0.033	1.957
Rmeas	0.154	0.033	1.987
Rpim	0.024	0.006	0.342
Total number of observations		25358	145969
Number of reflections	77616	809	4466
<I/σ(I)>	23.1	87.5	2.2
Completeness [%]	100.0	99.4	99.5
Redundancy	39.3	31.3	32.7
CC(1/2)	1.000	1.000	0.804

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289.15	0.25 uL ~6.6 mg/ml FphF+KT130 (0.2 mM KT130, 20% DMSO, 8 mM HEPES pH 7.5, 40 mM NaCl) were mixed with 0.2 uL of reservoir solution. Sitting drop reservoir contained 50 uL of 0.8 M sodium formate, 10% w/v PEG 8000, 10% w/v PEG 1000 and 0.1 M HEPES pH 7.0. Crystals were soaked for ~20 seconds in 75% reservoir solution and 25% glycerol prior to freezing in liquid nitrogen