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). |