9GG7

Crystal structure of 14-3-3 sigma dC - C38N in complex with Tau pS324 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	P 1 21 1
Unit cell lengths	69.240, 62.472, 69.291
Unit cell angles	90.00, 107.67, 90.00

Refinement procedure

Resolution	45.380 - 1.240
R-factor	0.2209
Rwork	0.220
R-free	0.24180
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	1.751
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.7.0009)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	65.970	1.260
High resolution limit [Å]	1.240	1.240
Number of reflections	344584	15878
<I/σ(I)>	7.7
Completeness [%]	97.5
Redundancy	4.4
CC(1/2)	0.981	0.414

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