8F1F

Structure of K48-linked tri-ubiquitin in complex with cyclic peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-06-03
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.0
Spacegroup name	P 1 2 1
Unit cell lengths	83.211, 26.963, 110.466
Unit cell angles	90.00, 99.85, 90.00

Refinement procedure

Resolution	30.000 - 1.850
R-factor	0.23137
Rwork	0.228
R-free	0.29813
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ubq monomer A
RMSD bond length	0.020
RMSD bond angle	2.107
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	1.880
High resolution limit [Å]	1.850	1.850
Rmeas	0.113	0.493
Rpim	0.061	0.263
Number of reflections	39731	2070
<I/σ(I)>	17.3
Completeness [%]	93.8	98.9
Redundancy	3.1	3.2
CC(1/2)	0.987	0.907

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	Droplets were formed by mixing equal volumes of Ub3:Ub4a complex (8 mg/ml) and the crystallization solution containing 0.15 M NaCl, 23% (w/v) PEG 3350 and 0.1 M HEPES (pH 7.5)