8V5U

Human SIRT3 bound to p53-AMC peptide and Honokiol

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALBA BEAMLINE XALOC
Synchrotron site	ALBA
Beamline	XALOC
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-06-02
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.979257
Spacegroup name	P 1 21 1
Unit cell lengths	34.452, 52.901, 68.753
Unit cell angles	90.00, 92.52, 90.00

Refinement procedure

Resolution	68.690 - 1.480
R-factor	0.2276
Rwork	0.226
R-free	0.24628
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.800
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]	68.690	1.500
High resolution limit [Å]	1.480	1.480
Number of reflections	40650	1828
<I/σ(I)>	11.9
Completeness [%]	97.9
Redundancy	3.4
CC(1/2)	0.997	0.754

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).