30TJ

14-3-3sigma protein binding to ERalpha-strong peptide (RSH mutation) and stabilizer 3'deAc FC-A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID30B
Synchrotron site	ESRF
Beamline	ID30B
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-02-16
Detector	DECTRIS EIGER2 X 9M
Wavelength(s)	0.873128
Spacegroup name	C 2 2 2
Unit cell lengths	59.950, 151.506, 75.997
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	75.997 - 2.150
Rwork	0.213
R-free	0.25450
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.218
Data reduction software	autoPROC
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0431 (refmacat 0.4.123))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	76.000	2.210
High resolution limit [Å]	2.150	2.150
Number of reflections	18393	1548
<I/σ(I)>	7.7	1.5
Completeness [%]	95.5
Redundancy	9.2
CC(1/2)	0.995	0.510

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		277	0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400