9FPM

Crystal structure of the Tin2-fold effector protein Tue1 from Thecaphora thlaspeos

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Synchrotron site	PETRA III, EMBL c/o DESY
Beamline	P13 (MX1)
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-09-23
Detector	DECTRIS EIGER R 1M
Wavelength(s)	0.97242
Spacegroup name	P 1
Unit cell lengths	38.050, 38.440, 39.470
Unit cell angles	114.53, 88.61, 119.66

Refinement procedure

Resolution	34.950 - 1.700
R-factor	0.1807
Rwork	0.179
R-free	0.21580
Structure solution method	SAD
RMSD bond length	0.006
RMSD bond angle	0.886
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.960	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.088	0.307
Number of reflections	18257	1793
<I/σ(I)>	13.51	4.35
Completeness [%]	95.7
Redundancy	7
CC(1/2)	0.997	0.979

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	294	0.05 M NaCl, 1.2M K/Na tartrate, 0.1M Imidazol