Small Angle Scattering Biological Data Bank SASBDB

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SASDA28 – anti-TG2 antibody (679 14 E06)

anti-TG2 antibody (679 14 E06) experimental SAS data

Sample:	Anti-TG2 antibody (679 14 E06) monomer, 48 kDa protein
Buffer:	20 mM Tris 150mM NaCl 1mM EDTA, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2015 Jan 17

Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease. J Biol Chem 290(35):21365-75 (2015)
Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM

R_g^Guinier	2.5	nm
D_max	8.1	nm
Volume^Porod	58	nm³

SASDA38 – transglutaminase-2 (TGA2)

transglutaminase 2 experimental SAS data

Sample:	Transglutaminase 2 monomer, 79 kDa Homo sapiens protein
Buffer:	20 mM Tris 150mM NaCl 1mM EDTA, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2015 Jan 17

R_g^Guinier	3.4	nm
D_max	12.0	nm
Volume^Porod	117	nm³

SASDA48 – transglutaminase2:anti-transglutaminase2 FAB1 antibody complex

anti-TG2 antibody (679 14 E06) transglutaminase 2 experimental SAS data

Sample:	Anti-TG2 antibody (679 14 E06) monomer, 48 kDa protein Transglutaminase 2 monomer, 79 kDa Homo sapiens protein
Buffer:	20 mM Tris 150mM NaCl 1mM EDTA, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2015 Jan 17

R_g^Guinier	4.0	nm
D_max	13.9	nm
Volume^Porod	168	nm³

SASDCJ2 – Solution structure of recombinant prion protein (89–230) in complex with Fab-P

Major prion proteinP-Clone Fab, Chimera experimental SAS data

Sample:	Major prion protein monomer, 23 kDa Mus musculus protein P-Clone Fab, Chimera monomer, 47 kDa Homo sapiens protein
Buffer:	sodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 mM NaCl), pH: 5.1
Experiment:	SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2013 Dec 5

Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. Biophys J 109(4):793-805 (2015)
Carter L, Kim SJ, Schneidman-Duhovny D, Stöhr J, Poncet-Montange G, Weiss TM, Tsuruta H, Prusiner SB, Sali A

R_g^Guinier	3.9	nm
D_max	14.5	nm
Volume^Porod	106	nm³

SASDAG7 – CD44 HABD scFv MEM-85 complex

Hyaluronate binding domain of CD44 antigenSingle-chain Variable Fragment of Antibody MEM-85 experimental SAS data

Sample:	Hyaluronate binding domain of CD44 antigen monomer, 18 kDa Homo sapiens protein Single-chain Variable Fragment of Antibody MEM-85 monomer, 29 kDa Mus musculus protein
Buffer:	PBS, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31

Molecular mechanism for the action of the anti-CD44 monoclonal antibody MEM-85. J Struct Biol 191(2):214-23 (2015)
Škerlová J, Král V, Kachala M, Fábry M, Bumba L, Svergun DI, Tošner Z, Veverka V, Řezáčová P

R_g^Guinier	2.7	nm
D_max	9.4	nm
Volume^Porod	57	nm³

SASDAD8 – Antiapoptotic membrane protein, (DpV84gp022) Deerpox virus

Antiapoptotic membrane protein experimental SAS data

Antiapoptotic membrane protein Kratky plot

Sample:	Antiapoptotic membrane protein dimer, 39 kDa Deerpox virus W-1170-84 protein
Buffer:	25 mM HEPES 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2013 May 4

Structural basis of Deerpox virus-mediated inhibition of apoptosis. Acta Crystallogr D Biol Crystallogr 71(Pt 8):1593-603 (2015)
Burton DR, Caria S, Marshall B, Barry M, Kvansakul M

R_g^Guinier	2.6	nm
D_max	11.1	nm
Volume^Porod	61	nm³

SASDAB8 – Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition).

PRKCA-binding protein experimental SAS data

Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition). Rg histogram

Sample:	PRKCA-binding protein dimer, 93 kDa Rattus norvegicus protein
Buffer:	50 mM Tris 125 mM NaCl 0.01 vol% reduced TX-100, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2015 May 11

Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering. Structure 23(7):1258-1270 (2015)
Karlsen ML, Thorsen TS, Johner N, Ammendrup-Johnsen I, Erlendsson S, Tian X, Simonsen JB, Høiberg-Nielsen R, Christensen NM, Khelashvili G, Streicher W, Teilum K, Vestergaard B, Weinstein H, Gether U, Arleth L, Madsen KL

R_g^Guinier	6.0	nm
D_max	20.0	nm
Volume^Porod	205	nm³

SASDA58 – UL26N of pseudorabies virus

Sample:	VP24 dimer, 53 kDa Suid herpesvirus 1 protein
Buffer:	50 mM Tris/HCl 0.5 M NaCl 0.25 M imidazole 5% glycerol 50 mM urea 0.2 M MgCl2, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23

Dimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine Protease. PLoS Pathog 11(7):e1005045 (2015)
Zühlsdorf M, Werten S, Klupp BG, Palm GJ, Mettenleiter TC, Hinrichs W

R_g^Guinier	2.6	nm
D_max	10.6	nm
Volume^Porod	73	nm³

SASDCL6 – Lys63-linked dimer ubiquitin

Sample:	Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Buffer:	100mM NaCl, 10mM sodium acetate, pH: 6
Experiment:	SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2016 Mar 24

Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition. Elife 4 (2015)
Liu Z, Gong Z, Jiang WX, Yang J, Zhu WK, Guo DC, Zhang WP, Liu ML, Tang C

R_g^Guinier	2.1	nm
D_max	6.5	nm
Volume^Porod	24	nm³

SASDAS7 – mouse olfactomedin-1

Sample:	Noelin tetramer, 256 kDa Mus musculus protein
Buffer:	20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2013 Nov 6

Olfactomedin-1 Has a V-shaped Disulfide-linked Tetrameric Structure. J Biol Chem 290(24):15092-101 (2015)
Pronker MF, Bos TG, Sharp TH, Thies-Weesie DM, Janssen BJ

R_g^Guinier	8.5	nm
D_max	30.0	nm
Volume^Porod	616	nm³

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