8ALO

Heterodimer formation of sensory domains of Vibrio cholerae regulators ToxR and ToxS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-12-08
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.967700
Spacegroup name	P 65
Unit cell lengths	72.507, 72.507, 79.463
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	62.793 - 3.002
Rwork	0.213
R-free	0.25290
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Alphafold Model
RMSD bond length	0.013
RMSD bond angle	1.749
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	62.793	62.790	3.180
High resolution limit [Å]	3.000	9.000	3.000
Rmerge	0.108	0.034	0.842
Rmeas	0.123	0.039	0.966
Rpim	0.059	0.018	0.466
Number of reflections	4790	183	756
<I/σ(I)>	12.8
Completeness [%]	100.0
Redundancy	8.1	7.6	7.8
CC(1/2)	0.999	0.999	0.688

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293.15	30mg/ml of ToxRSp in Tris buffer (20mM Tris, 150mM NaCl, pH7), 0.5 microliters of protein was mixed with 0.5 microliters of crystal condition (0.2 M Magnesium chloride hexahydrate. 0.1 M BIS-Tris. 5.5. 25 % w/v PEG 3350)