30TN

14-3-3sigma protein binding to ERalpha-strong peptide (RSH mutation)

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	2024-09-06
Detector	DECTRIS EIGER2 X 9M
Wavelength(s)	0.873128
Spacegroup name	C 2 2 21
Unit cell lengths	82.503, 112.053, 62.813
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.685 - 1.800
Rwork	0.158
R-free	0.18770
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.867
Data reduction software	autoPROC
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0431 (refmacat 0.4.126))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	66.440	1.840
High resolution limit [Å]	1.800	1.800
Number of reflections	27278	1602
<I/σ(I)>	14.7	4.5
Completeness [%]	99.8
Redundancy	8.6
CC(1/2)	0.998	0.898

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