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

SASDFU3 – Lysine-specific Demethylase (LSD2)

Lysyne-specific Demethylase LSD2
MWexperimental 90 kDa
MWexpected 89 kDa
VPorod 124 nm3
log I(s) 2.68×101 2.68×100 2.68×10-1 2.68×10-2
Lysyne-specific Demethylase LSD2 small angle scattering data  s, nm-1
ln I(s)
Lysyne-specific Demethylase LSD2 Guinier plot ln 2.69×101 Rg: 3.4 nm 0 (3.4 nm)-2 s2
Lysyne-specific Demethylase LSD2 Kratky plot 1.104 0 3 sRg
Lysyne-specific Demethylase LSD2 pair distance distribution function Rg: 3.4 nm 0 Dmax: 10.6 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of lysine-specific demethylase (LSD2) 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: 3 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the sample as a series of 167 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.

Lysyne-specific Demethylase LSD2 (LSD2)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   88.8 kDa
UniProt   Q8NB78 (31-822)
Sequence   FASTA