30TL

14-3-3sigma protein binding to ERalpha-weak peptide (AAA 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	81.864, 111.898, 62.747
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.540 - 1.200
Rwork	0.156
R-free	0.17760
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.024
RMSD bond angle	1.906
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]	66.070	1.220
High resolution limit [Å]	1.200	1.200
Number of reflections	89979	4379
<I/σ(I)>	10	1.6
Completeness [%]	100.0
Redundancy	13.7
CC(1/2)	0.996	0.603

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