SASBDB entries for UniProt ID: P02768

SASDLC4 – Human Albumin (HSA) Healthy donor used for HNA1, HNA2, HMA fractions

UniProt ID: P02768 (None-None) Albumin
Albumin experimental SAS data
Albumin Kratky plot
Sample: Albumin monomer, 69 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 1
Albumin in patients with liver disease shows an altered conformation. Commun Biol 4(1):731 (2021)
Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M
RgGuinier 2.8 nm
Dmax 8.5 nm

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

UniProt ID: P01308 (25-110) Insulin detemir (Levemir(R), Novo Nordisk A/S)

UniProt ID: P02768 (25-609) Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)
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

SASDL24 – Human Albumin (HMA)

UniProt ID: P02768 (None-None) Albumin
Albumin experimental SAS data
Albumin Kratky plot
Sample: Albumin monomer, 69 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 1
Albumin in patients with liver disease shows an altered conformation. Commun Biol 4(1):731 (2021)
Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M
RgGuinier 2.8 nm
Dmax 9.2 nm

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

UniProt ID: P01308 (25-110) Insulin detemir (Levemir(R), Novo Nordisk A/S)

UniProt ID: P02768 (25-609) Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)
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

SASDL34 – Human Albumin (HNA1)

UniProt ID: P02768 (None-None) Albumin
Albumin experimental SAS data
Albumin Kratky plot
Sample: Albumin monomer, 69 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 1
Albumin in patients with liver disease shows an altered conformation. Commun Biol 4(1):731 (2021)
Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M
RgGuinier 2.9 nm
Dmax 8.9 nm

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

UniProt ID: P02768 (25-609) Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)

UniProt ID: P01308 (None-None) Insulin detemir (Levemir(R), Novo Nordisk A/S)
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

SASDL44 – Human Albumin (HNA2)

UniProt ID: P02768 (None-None) Albumin
Albumin experimental SAS data
Albumin Kratky plot
Sample: Albumin monomer, 69 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 1
Albumin in patients with liver disease shows an altered conformation. Commun Biol 4(1):731 (2021)
Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M
RgGuinier 2.8 nm
Dmax 8.1 nm

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

UniProt ID: P02768 (25-609) Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.)

UniProt ID: P01308 (None-None) Insulin detemir (Levemir(R), Novo Nordisk A/S)
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

SASDLU3 – Human Albumin (C1)

UniProt ID: P02768 (None-None) Albumin
Albumin experimental SAS data
SREFLEX model
Sample: Albumin monomer, 69 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 1
Albumin in patients with liver disease shows an altered conformation. Commun Biol 4(1):731 (2021)
Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M
RgGuinier 2.7 nm
Dmax 8.2 nm

SASDE26 – Albumin-insulin degludec 1:12 complex

UniProt ID: P02768 (25-609) Human Albumin (Recombumin(R) Elite, Albumedix Ltd.)

UniProt ID: P01308 (25-110) Insulin degludec(Tresiba(R), Novo Nordisk A/S)
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