9FS4

Crystal structure of 14-3-3 sigma in complex with Tau pS214 peptide and covalent stabilizer LD12

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-12-01
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.972425
Spacegroup name	C 2 2 21
Unit cell lengths	82.343, 112.226, 62.420
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	66.390 - 1.600
R-factor	0.18256
Rwork	0.182
R-free	0.19776
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.894
Data reduction software	autoPROC
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (Refmac5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	66.390	1.630
High resolution limit [Å]	1.600	1.600
Number of reflections	35088	1884
<I/σ(I)>	27.4
Completeness [%]	91.1
Redundancy	1.9
CC(1/2)	1.000	0.967

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		277	10mg/mL 14-3-3sigma delta C, 1.5eq peptide, 0.095 M HEPES pH 7.1, 28% PEG400, 0.19 M CaCl2, 5% (v/v) glycerol compound soaked