8BSA

Vc1313-LBD bound to D-arginine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-04-22
Detector	DECTRIS PILATUS3 X 2M
Wavelength(s)	0.8731
Spacegroup name	P 1
Unit cell lengths	38.499, 44.557, 55.337
Unit cell angles	75.81, 84.49, 74.74

Refinement procedure

Resolution	37.120 - 1.900
Rwork	0.191
R-free	0.22450
Structure solution method	AB INITIO PHASING
RMSD bond length	0.007
RMSD bond angle	0.956
Data reduction software	XDS
Data scaling software	XDS
Phasing software	Arcimboldo
Refinement software	REFMAC (5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.120	1.968
High resolution limit [Å]	1.900	1.900
Rmerge	0.086
Rmeas	0.103
Rpim	0.055
Number of reflections	26099	2611
<I/σ(I)>	7.46
Completeness [%]	96.3
Redundancy	3.4
CC(1/2)	0.994	0.580

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.7	293	0.1 M Tris (base) bicine pH 8.6 - 8.8, 17 - 21% v/v PEG 500 MME, 8 - 10% w/v PEG 20000.Before setting up the drops 13 mg ml-1 Vc1313-LBD was mixed with 10 mM D-arginine from a 200 mM stock. The protein-ligand mixture was then mixed with reservoir solution in a 3:1 ratio. Before flash freezing the crystal in liquid nitrogen, the PEG concentrations were raised to 23% v/v PEG 500*MME, 12% w/v PEG 20000.