30TI

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

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 21
Unit cell lengths	82.241, 112.493, 62.853
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	56.310 - 1.500
Rwork	0.127
R-free	0.15450
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	1.402
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]	66.390	1.530
High resolution limit [Å]	1.500	1.500
Number of reflections	46995	2293
<I/σ(I)>	22.5	7.4
Completeness [%]	100.0
Redundancy	12.2
CC(1/2)	0.999	0.976

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