A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.

Marabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A, Cell Rep 27(2):387-399.e7 (2019) Europe PMC

SASDFV3 – Cytokine-like nuclear factor dehydrogenase domain, NPAC DH (NPAC delta-261)

NPAC dehydrogenase domain
MWexperimental 125 kDa
MWexpected 125 kDa
VPorod 167 nm3
log I(s) 1.40×101 1.40×100 1.40×10-1 1.40×10-2
NPAC dehydrogenase domain small angle scattering data  s, nm-1
ln I(s)
NPAC dehydrogenase domain Guinier plot ln 1.40×101 Rg: 3.5 nm 0 (3.5 nm)-2 s2
NPAC dehydrogenase domain Kratky plot 1.104 0 3 sRg
NPAC dehydrogenase domain pair distance distribution function Rg: 3.5 nm 0 Dmax: 11.0 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of the dehydrogenase domain from cytokine-like nuclear factor (NPAC delta-261) in 15 mM HEPES, 200 mM NaCl, pH 7.3 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20 °C using the following parameters: Column: Wyatt WTC-030N5; Flow rate: 0.25 mL/min; Sample injection concentration: 2.5 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the sample as a series of 173 x 1 second exposures. Each unsubtracted data frame was normalised to the intensity of the transmitted beam and radially averaged and the scattering of an appropriate solvent-blank was subtracted. The resulting subtracted frames were scaled and averaged to generate the final SAXS profile displayed in this entry.

NPAC dehydrogenase domain (NPAC DH)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   31.4 kDa
UniProt   Q49A26 (261-553)
Sequence   FASTA