8H0C

Structure of the thermolabile hemolysin from Vibrio alginolyticus (in complex with arachidonic acid)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL19U1
Synchrotron site	SSRF
Beamline	BL19U1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-10-06
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97852
Spacegroup name	P 1 21 1
Unit cell lengths	66.104, 72.888, 83.899
Unit cell angles	90.00, 101.60, 90.00

Refinement procedure

Resolution	64.750 - 1.980
R-factor	0.194
Rwork	0.193
R-free	0.22700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6jkz
RMSD bond length	0.010
RMSD bond angle	0.970
Data reduction software	XDS (Jan 10, 2022 (BUILT 20220220))
Data scaling software	Aimless (0.5.29)
Phasing software	PHASER (2.7.17)
Refinement software	BUSTER (2.10.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	64.754	2.014
High resolution limit [Å]	1.980	1.980
Rmeas	0.094	0.998
Rpim	0.037	0.385
Number of reflections	54484	2731
<I/σ(I)>	13.8	2.1
Completeness [%]	99.9	99.9
Redundancy	6.5	6.6
CC(1/2)	0.998	0.767

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	The crystal of ValTLH in complex with arachidonic acid was grown in a drop containing 1.0 ul of protein solution (6 mg/ml in the buffer 10 mM HEPES pH 7.5, 150 mM NaCl, 1 mM DTT, 300mM NDSB201 with 1.25 mM arachidonic acid) and 1.0 ul of reservoir solution (25% polyethylene glycol 20000, 0.15 M magnesium formate).