8V15

Human SIRT3 bound to p53-AMC peptide, Carba-NAD, and Honokiol

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-06-02
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.9786
Spacegroup name	P 1 21 1
Unit cell lengths	34.683, 159.432, 53.047
Unit cell angles	90.00, 90.61, 90.00

Refinement procedure

Resolution	44.160 - 2.400
R-factor	0.19947
Rwork	0.194
R-free	0.30262
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	2.914
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.160	2.440
High resolution limit [Å]	2.400	2.400
Number of reflections	21620	964
<I/σ(I)>	10.4
Completeness [%]	96.2
Redundancy	3.1
CC(1/2)	0.983	0.807

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION		293.15	SIRT3 (118-399) (10.3 mg/ml) was crystallized in complex with FDL (QPKKAC-7-amino-4-methylcoumarin) peptide (3 mM) and honokiol (1 mM) in 25% PEG 3350, 0.2 M Li2SO4 (or 0.2 M NaCl), and 0.1M HEPES, pH 7.5 as reservoir. Following formation of the ternary complex, crystals were soaked with carba-NAD (10 mM).