Small Angle Scattering Biological Data Bank SASBDB

SASDBP2 – Human linear triubiquitin

Human linear tri-ubiquitin experimental SAS data

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

New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
Thach TT, Shin D, Han S, Lee S

R_g^Guinier	2.5	nm
D_max	8.6	nm
Volume^Porod	36	nm³

SASDBQ2 – Human linear tetraubiquitin

Human linear tetra-ubiquitin experimental SAS data

Human linear tetraubiquitin Rg histogram

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

R_g^Guinier	3.1	nm
D_max	11.2	nm
Volume^Porod	49	nm³

SASDMU4 – Retinoic acid receptor RXR-alpha ligand binding domain (LBD)

Retinoic acid receptor RXR-alpha experimental SAS data

Sample:	Retinoic acid receptor RXR-alpha dimer, 51 kDa Homo sapiens protein
Buffer:	20 mM Tris, 100 mM NaCl, 100 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 7

Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N

R_g^Guinier	2.5	nm
D_max	8.3	nm
Volume^Porod	60	nm³

SASDMV4 – Full-length Retinoic acid receptor RXR-alpha in complex with Ramp2 DNA

Retinoic acid receptor RXR-alphaRamp2 DNA experimental SAS data

Sample:	Retinoic acid receptor RXR-alpha dimer, 102 kDa Homo sapiens protein Ramp2 DNA monomer, 11 kDa DNA
Buffer:	20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 May 7

R_g^Guinier	4.4	nm
D_max	13.9	nm
Volume^Porod	161	nm³

SASDMW4 – Retinoic acid receptor RXR-alpha N-terminal and DNA binding domains (DBD) in complex with Ramp2 DNA

Ramp2 DNARetinoic acid receptor RXR-alpha experimental SAS data

Sample:	Ramp2 DNA monomer, 11 kDa DNA Retinoic acid receptor RXR-alpha dimer, 44 kDa Homo sapiens protein
Buffer:	20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Jul 17

R_g^Guinier	4.3	nm
D_max	14.3	nm
Volume^Porod	89	nm³

SASDMX4 – Retinoic acid receptor RXR-alpha DNA binding (DBD) and ligand binding (LBD) domains in complex with Ramp2 DNA

Sample:	Ramp2 DNA monomer, 11 kDa DNA Retinoic acid receptor RXR-alpha dimer, 74 kDa Homo sapiens protein
Buffer:	20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 7

R_g^Guinier	3.6	nm
D_max	12.2	nm

SASDMY4 – Retinoic acid receptor RXR-alpha DNA binding domain (DBD) in complex with Ramp2

Sample:	Ramp2 DNA monomer, 11 kDa DNA Retinoic acid receptor RXR-alpha dimer, 20 kDa Homo sapiens protein
Buffer:	20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 7

R_g^Guinier	1.9	nm
D_max	5.8	nm

SASDBR2 – Contactin-associated protein-like 2 (Caspr2) extracellular domains 1-1261.

Contactin-associated protein-like 2 extracellular domains (1-1261) experimental SAS data

Sample:	Contactin-associated protein-like 2 extracellular domains (1-1261) monomer, 140 kDa Homo sapiens protein
Buffer:	10 mM HEPES 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at Anton Paar SAXSess, University of Utah on 2010 Oct 4

Structural Characterization of the Extracellular Domain of CASPR2 and Insights into Its Association with the Novel Ligand Contactin1. J Biol Chem 291(11):5788-802 (2016)
Rubio-Marrero EN, Vincelli G, Jeffries CM, Shaikh TR, Pakos IS, Ranaivoson FM, von Daake S, Demeler B, De Jaco A, Perkins G, Ellisman MH, Trewhella J, Comoletti D

R_g^Guinier	4.4	nm
D_max	14.5	nm
Volume^Porod	282	nm³

SASDAX8 – Ribokinase ThiM

Sample:	Ribokinase ThiM trimer, 89 kDa Staphylococcus aureus protein
Buffer:	50 mM Potassium phosphate 10 mM MgCl2, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 19

Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections. Sci Rep 6:22871 (2016)
Drebes J, Künz M, Windshügel B, Kikhney AG, Müller IB, Eberle RJ, Oberthür D, Cang H, Svergun DI, Perbandt M, Betzel C, Wrenger C

R_g^Guinier	3.0	nm
D_max	9.0	nm
Volume^Porod	145	nm³

SASDAD7 – Structure of a complex between full length and truncated CTP1L endolysin

Sample:	Endolysin , 33 kDa Clostridium phage phiCTP1 protein
Buffer:	20 mM HEPES, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 17

Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product. J Biol Chem 291(10):4882-93 (2016)
Dunne M, Leicht S, Krichel B, Mertens HD, Thompson A, Krijgsveld J, Svergun DI, Gómez-Torres N, Garde S, Uetrecht C, Narbad A, Mayer MJ, Meijers R

R_g^Guinier	3.7	nm
D_max	13.8	nm
Volume^Porod	95	nm³

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