Small Angle Scattering Biological Data Bank SASBDB

SASDA65 – Nucleoplasmin-H5 complex

Sample:	NP-H5 pentamer, 200 kDa Escherichia coli protein
Buffer:	20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Dec 3

A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models. J Mol Biol 393(2):448-63 (2009)
Taneva SG, Bañuelos S, Falces J, Arregi I, Muga A, Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA

R_g^Guinier	5.2	nm
D_max	16.7	nm
Volume^Porod	410	nm³

SASDA75 – Nucleoplasmin-H2AH2B complex

Sample:	NP-H2AH2B pentamer, 250 kDa Escherichia coli protein
Buffer:	20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2014 Dec 3

R_g^Guinier	4.7	nm
D_max	14.5	nm
Volume^Porod	470	nm³

SASDAH4 – DH-PH

DH-PH module of PDZRhoGEF experimental SAS data

Sample:	DH-PH module of PDZRhoGEF monomer, 41 kDa Homo sapiens protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Oct 30

The solution structure and dynamics of the DH-PH module of PDZRhoGEF in isolation and in complex with nucleotide-free RhoA. Protein Sci 18(10):2067-79 (2009)
Cierpicki T, Bielnicki J, Zheng M, Gruszczyk J, Kasterka M, Petoukhov M, Zhang A, Fernandez EJ, Svergun DI, Derewenda U, Bushweller JH, Derewenda ZS

R_g^Guinier	2.9	nm
D_max	9.0	nm
Volume^Porod	60	nm³

SASDAQ4 – 6:3 complex of GAD:CaM

CalmodulinGlutamate decarboxylase experimental SAS data

Sample:	Calmodulin monomer, 17 kDa Homo sapiens protein Glutamate decarboxylase hexamer, 340 kDa Petunia x hybrida protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Nov 9

A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. J Mol Biol 392(2):334-51 (2009)
Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G

R_g^Guinier	5.9	nm
D_max	23.0	nm
Volume^Porod	630	nm³

SASDAS3 – Fila16-17

immunoglobulin- like filamin two-domain fragment 16-17 experimental SAS data

Sample:	immunoglobulin- like filamin two-domain fragment 16-17 monomer, 19 kDa Escherichia coli protein
Buffer:	100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18

Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J

R_g^Guinier	1.9	nm
D_max	6.0	nm
Volume^Porod	33	nm³

SASDAT3 – Fila18-19

immunoglobulin- like filamin two-domain fragment 18-19 experimental SAS data

Sample:	immunoglobulin- like filamin two-domain fragment 18-19 monomer, 20 kDa Escherichia coli protein
Buffer:	100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18

R_g^Guinier	2.1	nm
D_max	6.5	nm
Volume^Porod	34	nm³

SASDAU3 – Fila22-23

immunoglobulin- like filamin two-domain fragment 22-23 experimental SAS data

Sample:	immunoglobulin- like filamin two-domain fragment 22-23 monomer, 19 kDa Escherichia coli protein
Buffer:	100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18

R_g^Guinier	2.8	nm
D_max	9.0	nm
Volume^Porod	32	nm³

SASDN33 – Ternary Human Pex5p(C-terminal)-Pex14p(N)-PTS1 Complex (1:1:1 stoichiometry)

Peroxisomal targeting signal 1 receptor (C -terminal)Peroxisomal membrane protein PEX14 (N-terminal)PTS1-BP experimental SAS data

Sample:	Peroxisomal targeting signal 1 receptor (C -terminal) monomer, 48 kDa Homo sapiens protein Peroxisomal membrane protein PEX14 (N-terminal) monomer, 7 kDa Homo sapiens protein PTS1-BP monomer, 14 kDa Homo sapiens protein
Buffer:	50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Oct 3

Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284(37):25334-42 (2009)
Shiozawa K, Konarev PV, Neufeld C, Wilmanns M, Svergun DI

R_g^Guinier	2.9	nm
D_max	9.0	nm
Volume^Porod	110	nm³

SASDN43 – Full-length Human Pex5p protein

Peroxisomal targeting signal 1 receptor experimental SAS data

Sample:	Peroxisomal targeting signal 1 receptor monomer, 71 kDa Homo sapiens protein
Buffer:	50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Feb 24

R_g^Guinier	5.0	nm
D_max	20.0	nm
Volume^Porod	181	nm³

SASDN53 – Ternary Human Pex5p(full-length)-Pex14p(N)-PTS1 Protein Complex (1:7:1 stoichiometry)

Peroxisomal targeting signal 1 receptorPeroxisomal membrane protein PEX14PTS1-BP experimental SAS data

Sample:	Peroxisomal targeting signal 1 receptor monomer, 71 kDa Homo sapiens protein Peroxisomal membrane protein PEX14 monomer, 7 kDa Homo sapiens protein PTS1-BP monomer, 13 kDa Homo sapiens protein
Buffer:	50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Mar 18

R_g^Guinier	6.0	nm
D_max	20.0	nm
Volume^Porod	267	nm³

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