9S1S

Crystal structure of C278S mutant of mouse CDC14A in complex with a model phosphopeptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX IV BEAMLINE BioMAX
Synchrotron site	MAX IV
Beamline	BioMAX
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-12-05
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.72931
Spacegroup name	C 1 2 1
Unit cell lengths	102.342, 158.093, 69.274
Unit cell angles	90.00, 124.59, 90.00

Refinement procedure

Resolution	28.820 - 1.620
R-factor	0.1698
Rwork	0.168
R-free	0.20670
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.009
RMSD bond angle	0.906
Data reduction software	autoPROC
Data scaling software	Aimless
Phasing software	PHENIX (1.21rc1_5127)
Refinement software	PHENIX (1.21rc1_5127)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	79.050	1.780
High resolution limit [Å]	1.620	1.720
Rmerge	0.117	1.585
Rmeas	0.127	0.127
Rpim	0.047	0.628
Number of reflections	79380	3969
<I/σ(I)>	9.9	1.5
Completeness [%]	69.2
Redundancy	7.2
CC(1/2)	0.996	0.452

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	0.2M sodium sulphate; polymer: 20% (w/v) polyethylene glycol 3350; Buffer: 0.1M Bis-Tris propane, pH 7.5