9GG8

Crystal structure of 14-3-3 sigma dC - C38N in complex with Tau pS214 peptide and covalent stabilizer 187

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-06-04
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.96546
Spacegroup name	C 2 2 21
Unit cell lengths	82.254, 112.509, 62.482
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	66.400 - 1.100
R-factor	0.1986
Rwork	0.199
R-free	0.20250
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	1.653
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.7.0009)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	66.400	1.120
High resolution limit [Å]	1.100	1.100
Number of reflections	743401	35764
<I/σ(I)>	13.7
Completeness [%]	99.9
Redundancy	6.3
CC(1/2)	0.990	0.719

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		277	Cocrystalization of 12 mg/ml protein, 2eq peptide and 1.8mM compound in 20 mM Sodium HEPES pH 7.5, 2 mM MgCl2, and 1.5 mM TCEP. Crystallization buffer: 0.19 M Calcium chloride dihydrate, 0.095 M Sodium HEPES pH 7.1, 5% glycerol, and28% PEG 400, mixed 1:1 with cocrystal mix