9NEM

Structure of Unc119-Farnesylated peptide complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CMOS
Collection date	2023-10-10
Detector	RDI CMOS_8M
Wavelength(s)	1.07
Spacegroup name	P 21 21 21
Unit cell lengths	79.159, 81.039, 192.330
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.820 - 2.490
R-factor	0.2646
Rwork	0.263
R-free	0.29490
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.551
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	PHENIX (1.21.1_5286)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.820	2.580
High resolution limit [Å]	2.490	2.490
Number of reflections	43838	4570
<I/σ(I)>	11.7
Completeness [%]	99.1
Redundancy	6.3
CC(1/2)	0.995	0.734

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277	100 mM sodium acetate, pH 4.5-5.5, 200 mM ammonium acetate, 20-30% PEG4000