Browse by ORGANISM: other species

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
DAMFILT model
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
RgGuinier 1.7 nm
Dmax 5.4 nm
VolumePorod 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
PDB (PROTEIN DATA BANK) model
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
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
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 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
OTHER model
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
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
RgGuinier 3.7 nm
Dmax 11.1 nm
VolumePorod 101 nm3

SASDEV5 – Insulin detemir tri-hexamer

Insulin detemir experimental SAS data
SASREF CV model
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
RgGuinier 3.3 nm
Dmax 11.3 nm
VolumePorod 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
SASREF CV model
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
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
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 162 nm3

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

Insulin detemir (Levemir(R), Novo Nordisk A/S)Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.) experimental SAS data
SASREF CV model
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
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
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 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
SASREF CV model
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
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
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 309 nm3

SASDEZ5 – Albumin-insulin detemir 2:12 complex, P2 symmetry

Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)Insulin detemir (Levemir(R), Novo Nordisk A/S) experimental SAS data
SASREF CV model
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
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
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 309 nm3

SASDE26 – Albumin-insulin degludec 1:12 complex

Human Albumin (Recombumin(R) Elite, Albumedix Ltd.)Insulin degludec(Tresiba(R), Novo Nordisk A/S) experimental SAS data
SASREF CV model
Sample: Human Albumin (Recombumin(R) Elite, Albumedix Ltd.) monomer, 66 kDa protein
Insulin degludec(Tresiba(R), Novo Nordisk A/S) dodecamer, 73 kDa protein
Buffer: 25 mM Na2HPO4, 15.9 mM m-cresol, 15.9 mM phenol, 212.8 mM glycerol, 20 mM NaCl, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 27
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
RgGuinier 3.8 nm
Dmax 13.4 nm
VolumePorod 179 nm3

SASDE48 – Toxin GraT

Putative killer protein, Toxin GraT. experimental SAS data
Putative killer protein, Toxin GraT. Kratky plot
Sample: Putative killer protein, Toxin GraT. monomer, 11 kDa Pseudomonas putida protein
Buffer: 50 mM Tris 250 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Sep 21
A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. Nat Commun 10(1):972 (2019)
Talavera A, Tamman H, Ainelo A, Konijnenberg A, Hadži S, Sobott F, Garcia-Pino A, Hõrak R, Loris R
RgGuinier 1.5 nm
Dmax 5.5 nm
VolumePorod 18 nm3