Small Angle Scattering Biological Data Bank SASBDB

Browse by MACROMOLECULE type: protein

SASDDF3 – Macrophage migration inhibitory factor bound to Ceruloplasmin (MIF-CP complex)

Macrophage migration inhibitory factorCeruloplasmin experimental SAS data

Sample:	Macrophage migration inhibitory factor trimer, 37 kDa Homo sapiens protein Ceruloplasmin monomer, 122 kDa Homo sapiens protein
Buffer:	50mkm CuSO4, 100mM Hepes, pH: 7.4
Experiment:	SAXS data collected at HECUS System-3, None on 2015 Dec 22

Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor. Biochemistry (Mosc) 83(6):701-707 (2018)
Sokolov AV, Dadinova LA, Petoukhov MV, Bourenkov G, Dubova KM, Amarantov SV, Volkov VV, Kostevich VA, Gorbunov NP, Grudinina NA, Vasilyev VB, Samygina VR

R_g^Guinier	3.6	nm
D_max	14.4	nm
Volume^Porod	228	nm³

SASDDS4 – cGMP-dependent protein kinase 1: ∆53 PKG Iα

cGMP-dependent protein kinase 1 experimental SAS data

Sample:	CGMP-dependent protein kinase 1 monomer, 70 kDa Bos taurus protein
Buffer:	50 mM MES, 300 mM NaCl, 1 mM TCEP, 5 mM DTT, pH: 6.9
Experiment:	SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Jun 6

An N-terminally truncated form of cyclic GMP-dependent protein kinase Iα (PKG Iα) is monomeric and autoinhibited and provides a model for activation. J Biol Chem 293(21):7916-7929 (2018)
Moon TM, Sheehe JL, Nukareddy P, Nausch LW, Wohlfahrt J, Matthews DE, Blumenthal DK, Dostmann WR

R_g^Guinier	3.0	nm
D_max	9.7	nm
Volume^Porod	105	nm³

SASDDU5 – Nonstructural protein sigma NS - apoprotein

Nonstructural protein sigma NS experimental SAS data

Nonstructural protein sigma NS Kratky plot

Sample:	Nonstructural protein sigma NS hexamer, 244 kDa Avian orthoreovirus protein
Buffer:	25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Feb 25

Stability of local secondary structure determines selectivity of viral RNA chaperones. Nucleic Acids Res (2018)
Bravo JPK, Borodavka A, Barth A, Calabrese AN, Mojzes P, Cockburn JJB, Lamb DC, Tuma R

R_g^Guinier	5.5	nm
D_max	23.1	nm
Volume^Porod	670	nm³

SASDD46 – Artificially designed de novo protein esPN-Block (HL4) heterocomplex, e1s2 (HL4)

extender PN-Block (HL4)stopper PN-Block (WA20) experimental SAS data

Sample:	Extender PN-Block (HL4) monomer, 27 kDa de novo protein protein Stopper PN-Block (WA20) dimer, 25 kDa de novo protein protein
Buffer:	20 mM HEPES, 100 mM NaCl, 200 mM ArgHCl, 10% glycerol, pH: 7.5
Experiment:	SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2014 Dec 19

Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks. ACS Synth Biol 7(5):1381-1394 (2018)
Kobayashi N, Inano K, Sasahara K, Sato T, Miyazawa K, Fukuma T, Hecht MH, Song C, Murata K, Arai R

R_g^Guinier	3.6	nm
D_max	15.0	nm

SASDD56 – Artificially designed de novo protein esPN-Block (FL4) heterocomplex, e1s2 (FL4)

stopper PN-Block (WA20)extender PN-Block (FL4) experimental SAS data

Sample:	Stopper PN-Block (WA20) dimer, 25 kDa de novo protein protein Extender PN-Block (FL4) monomer, 27 kDa de novo protein protein
Buffer:	20 mM HEPES, 100 mM NaCl, 200 mM ArgHCl, 10% glycerol, pH: 7.5
Experiment:	SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2014 Dec 19

R_g^Guinier	3.3	nm
D_max	12.0	nm

SASDB43 – Human dystrophin central domain repeats 1 to 2

Dystrophin central domain repeats 1 to 2 experimental SAS data

Sample:	Dystrophin central domain repeats 1 to 2 monomer, 26 kDa Homo sapiens protein
Buffer:	20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2011 Oct 7

Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E

R_g^Guinier	3.0	nm
D_max	10.6	nm
Volume^Porod	42	nm³

SASDB53 – Human dystrophin central domain repeats 1 to 3

Dystrophin central domain repeats 1 to 3 experimental SAS data

Sample:	Dystrophin central domain repeats 1 to 3 monomer, 38 kDa Homo sapiens protein
Buffer:	20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2011 Sep 9

R_g^Guinier	4.2	nm
D_max	17.0	nm
Volume^Porod	68	nm³

SASDB63 – Human dystrophin central domain repeats 11 to 15

Dystrophin central domain repeats 11 to 15. experimental SAS data

Sample:	Dystrophin central domain repeats 11 to 15. monomer, 60 kDa Homo sapiens protein
Buffer:	20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2011 Apr 11

R_g^Guinier	5.8	nm
D_max	23.0	nm
Volume^Porod	87	nm³

SASDB73 – Human dystrophin central domain repeats 4 to 9

Dystrophin central domain repeats 4 to 9 experimental SAS data

Sample:	Dystrophin central domain repeats 4 to 9 monomer, 76 kDa Homo sapiens protein
Buffer:	20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2012 Sep 19

R_g^Guinier	7.7	nm
D_max	30.5	nm
Volume^Porod	123	nm³

SASDB83 – Human dystrophin central domain repeats 16 to 17

Dystrophin central domain repeats 16 to 17. experimental SAS data

Sample:	Dystrophin central domain repeats 16 to 17. monomer, 28 kDa Homo sapiens protein
Buffer:	20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2012 Sep 19

R_g^Guinier	3.1	nm
D_max	13.0	nm
Volume^Porod	47	nm³

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