New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin.

Thach TT, Shin D, Han S, Lee S
Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016 Apr)

PMID: 27050132 doi: 10.1107/S2059798316001510

Submitted to SASBDB: 2015 Oct 16 Published in SASBDB: 2016 Apr 7

SASDBN2 – Human linear diubiquitin Sample: Linear di-ubiquitin monomer, 17 kDa Homo sapiens protein Buffer: 50 mM Tris 150 mM NaCl 1 mM MgCl2, pH: 7.5 Experiment: SAXS data collected at 5C, Pohang Accelerator Laboratory on 2014 Nov 3 RgGuinier 2.1 nm Dmax 6.6 nm VolumePorod 20 nm3

SASDBP2 – Human linear triubiquitin Sample: Human linear tri-ubiquitin monomer, 26 kDa Homo sapiens protein Buffer: 50 mM Tris 150mM NaCl 0.5 mM EDTA, pH: 7.5 Experiment: SAXS data collected at 5C, Pohang Accelerator Laboratory on 2014 Nov 3 RgGuinier 2.5 nm Dmax 8.6 nm VolumePorod 36 nm3

SASDBQ2 – Human linear tetraubiquitin Sample: Human linear tetra-ubiquitin monomer, 34 kDa Homo sapiens protein Buffer: 50 mM Tris 150mM NaCl 0.5 mM EDTA, pH: 7.5 Experiment: SAXS data collected at 5C, Pohang Accelerator Laboratory on 2014 Nov 3 RgGuinier 3.1 nm Dmax 11.2 nm VolumePorod 49 nm3