8H09

Structure of the thermolabile hemolysin from Vibrio alginolyticus (apo form)

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	2019-11-11
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97876
Spacegroup name	P 1 21 1
Unit cell lengths	65.932, 71.238, 83.645
Unit cell angles	90.00, 101.32, 90.00

Refinement procedure

Resolution	53.780 - 1.810
R-factor	0.181
Rwork	0.180
R-free	0.20400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6jkz
RMSD bond length	0.010
RMSD bond angle	0.930
Data reduction software	XDS (Mar 15, 2019, built on 20190315)
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]	53.783	1.840
High resolution limit [Å]	1.809	1.809
Rmeas	0.087	0.767
Rpim	0.033	0.288
Number of reflections	68600	3412
<I/σ(I)>	12.9	2.3
Completeness [%]	98.8	98.1
Redundancy	6.9	6.9
CC(1/2)	0.998	0.863

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	The crystal of ValTLH was grown in a drop containing 1.0 ul of protein solution (10 mg/ml in the buffer 10 mM HEPES pH 7.5, 150 mM NaCl, 1 mM DTT, 200 mM NDSB201) and 1.0 ul of reservoir solution (0.1 M Tris pH 8.5, 20.5% polyethylene glycol 4000, 20% polyethylene glycol 400, and 0.1 M MgCl2).