Small Angle Scattering Biological Data Bank SASBDB

Browse by MACROMOLECULE type: protein

SASDKP2 – Matrix protein from Newcastle disease virus at acidic pH

Sample:	Matrix protein dimer, 79 kDa Newcastle disease virus … protein
Buffer:	STE buffer 100 mM NaCl, 10 mM Tris-HCl, and 1 mM EDTA, pH: 4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Dec 11

Solution Structure, Self-Assembly, and Membrane Interactions of the Matrix Protein from Newcastle Disease Virus at Neutral and Acidic pH Journal of Virology 93(6) (2019)
Shtykova E, Petoukhov M, Dadinova L, Fedorova N, Tashkin V, Timofeeva T, Ksenofontov A, Loshkarev N, Baratova L, Jeffries C, Svergun D, Batishchev O, García-Sastre A

R_g^Guinier

3.3

SASDC28 – Mature α-DsbA2 protein

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data

Sample:	DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) trimer, 81 kDa Wolbachia endosymbiont of … protein
Buffer:	25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2014 Mar 29

The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase. Acta Crystallogr D Struct Biol 75(Pt 3):283-295 (2019)
Walden PM, Whitten AE, Premkumar L, Halili MA, Heras B, King GJ, Martin JL

R_g^Guinier	2.8	nm
D_max	8.7	nm
Volume^Porod	913	nm³

SASDC38 – Truncated α-DsbA2 protein

Sample:	DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) monomer, 21 kDa Wolbachia endosymbiont of … protein
Buffer:	25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29

R_g^Guinier	1.9	nm
D_max	6.3	nm
Volume^Porod	275	nm³

SASDEK4 – C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein (ScsC)

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein experimental SAS data

Sample:	C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein monomer, 20 kDa Proteus mirabilis protein
Buffer:	10mM HEPES, 150mM NaCl, pH: 7.4
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5

Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis. Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019)
Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL

R_g^Guinier	1.7	nm
D_max	5.4	nm
Volume^Porod	22200	nm³

SASDEQ4 – Deletion mutant of the suppressor of copper sensitivity C protein, PmScsC, with concentration series data

Deletion mutant of PmScsC experimental SAS data

Sample:	Deletion mutant of PmScsC, 23 kDa Proteus mirabilis protein
Buffer:	10mM HEPES, 150mM NaCl, pH: 7.4
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5

R_g^Guinier	2.6	nm
D_max	9.0	nm
Volume^Porod	54	nm³

SASDER4 – Wild-type suppressor of copper sensitivity C protein, PmScsC, with concentration series data

Suppressor of Copper Sensitivity C protein experimental SAS data

Sample:	Suppressor of Copper Sensitivity C protein trimer, 74 kDa Proteus mirabilis protein
Buffer:	10mM HEPES, 150mM NaCl, pH: 7.4
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5

R_g^Guinier	3.7	nm
D_max	11.1	nm
Volume^Porod	101	nm³

SASDEV5 – Insulin detemir tri-hexamer

Sample:	Insulin detemir 18-mer, 106 kDa protein
Buffer:	5.0 mM Na2HPO4, 13.1 mM m-cresol, 15.1 mM phenol, 173.7 mM glycerol, 20.0 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at I911-4, MAX IV on 2015 Sep 25

Solution structures of long-acting insulin analogues and their complexes with albumin. Acta Crystallogr D Struct Biol 75(Pt 3):272-282 (2019)
Ryberg LA, Sønderby P, Barrientos F, Bukrinski JT, Peters GHJ, Harris P

R_g^Guinier	3.3	nm
D_max	11.3	nm
Volume^Porod	137	nm³

SASDEW5 – Albumin-insulin detemir 1:6 complex, binding in Südlow's Site II

Insulin detemir (Levemir(R), Novo Nordisk A/S)Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.) experimental SAS data

Sample:	Insulin detemir (Levemir(R), Novo Nordisk A/S) hexamer, 35 kDa protein Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.) monomer, 66 kDa protein
Buffer:	6.9 mM Na2HPO4, 11.9 mM m-cresol, 13.7 mM phenol, 157.3 mM glycerol, 38.5 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at I911-4, MAX IV on 2015 Sep 25

R_g^Guinier	3.5	nm
D_max	13.0	nm
Volume^Porod	162	nm³

SASDEX5 – Albumin-insulin detemir 1:6 complex, binding in Südlow's Site I

Sample:	Insulin detemir (Levemir(R), Novo Nordisk A/S) hexamer, 35 kDa protein Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.) monomer, 66 kDa protein
Buffer:	6.9 mM Na2HPO4, 11.9 mM m-cresol, 13.7 mM phenol, 157.3 mM glycerol, 38.5 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at I911-4, MAX IV on 2015 Sep 25

R_g^Guinier	3.5	nm
D_max	13.0	nm
Volume^Porod	162	nm³

SASDEY5 – Albumin-insulin detemir 2:12 complex, P1 symmetry

Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)Insulin detemir (Levemir(R), Novo Nordisk A/S) experimental SAS data

Sample:	Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.) monomer, 66 kDa protein Insulin detemir (Levemir(R), Novo Nordisk A/S) dodecamer, 71 kDa protein
Buffer:	8.8 mM Na2HPO4, 10.6 mM m-cresol, 12.2 mM phenol, 140.9 mM glycerol, 56.9 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at I911-4, MAX IV on 2015 Sep 25

R_g^Guinier	5.4	nm
D_max	19.5	nm
Volume^Porod	309	nm³

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