Structural insights into the C-terminus of the histone-lysine N-methyltransferase NSD3 by small-angle X-ray scattering.

Belviso BD, Shen Y, Carrozzini B, Morishita M, di Luccio E, Caliandro R
Front Mol Biosci 11:1191246 (2024)
PMID: 38516186
doi: 10.3389/fmolb.2024.1191246 		Submitted to SASBDB: 2022 Apr 22
Published in SASBDB:

SASDNL8 – The C-terminal region of histone-lysine N-methyltransferase NSD3: PWWP2-SET construct

Histone-lysine N-methyltransferase NSD3 experimental SAS data
OTHER model
Sample: Histone-lysine N-methyltransferase NSD3 monomer, 43 kDa Homo sapiens protein
Buffer: 0.5 M NaCl, 20 mM Tris-HCl, 5 mM DTT, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Nov 25
RgGuinier 3.1 nm
Dmax 11.2 nm
VolumePorod 64 nm3

SASDNK8 – The C-terminal region of histone-lysine N-methyltransferase NSD3: SET-PHD4 construct

Histone-lysine N-methyltransferase NSD3 experimental SAS data
OTHER model
Sample: Histone-lysine N-methyltransferase NSD3 monomer, 40 kDa Homo sapiens protein
Buffer: 0.5 M NaCl, 20 mM Tris-HCl, 5 mM DTT, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Nov 25
RgGuinier 3.4 nm
Dmax 13.2 nm
VolumePorod 75 nm3