SASBDB entries for UniProt ID:

SASDJC3 – Ubiquitin carboxyl-terminal hydrolase, MINDY2 (C266A mutant), bound to tri-ubiquitin

UniProt ID: Q8NBR6 (241-504) Ubiquitin carboxyl-terminal hydrolase C266A mutant

UniProt ID: P0CG48 (1-76) Polyubiquitin-C
Ubiquitin carboxyl-terminal hydrolase C266A mutantPolyubiquitin-C experimental SAS data
CUSTOM IN-HOUSE model
Sample: Ubiquitin carboxyl-terminal hydrolase C266A mutant monomer, 31 kDa Homo sapiens protein
Polyubiquitin-C trimer, 26 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 26
Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2. Mol Cell (2021)
Abdul Rehman SA, Armstrong LA, Lange SM, Kristariyanto YA, Gräwert TW, Knebel A, Svergun DI, Kulathu Y
RgGuinier 2.8 nm
Dmax 8.8 nm
VolumePorod 97 nm3

SASDJD3 – Ubiquitin carboxyl-terminal hydrolase, MINDY2 (C266A mutant), bound to tetra-ubiquitin

UniProt ID: Q8NBR6 (241-504) Ubiquitin carboxyl-terminal hydrolase C266A mutant

UniProt ID: P0CG48 (1-76) Polyubiquitin-C
Ubiquitin carboxyl-terminal hydrolase C266A mutantPolyubiquitin-C experimental SAS data
CUSTOM IN-HOUSE model
Sample: Ubiquitin carboxyl-terminal hydrolase C266A mutant monomer, 31 kDa Homo sapiens protein
Polyubiquitin-C tetramer, 34 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 26
Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2. Mol Cell (2021)
Abdul Rehman SA, Armstrong LA, Lange SM, Kristariyanto YA, Gräwert TW, Knebel A, Svergun DI, Kulathu Y
RgGuinier 2.9 nm
Dmax 9.2 nm
VolumePorod 111 nm3

SASDJE3 – Ubiquitin carboxyl-terminal hydrolase, MINDY2 (C266A mutant), bound to penta-ubiquitin

UniProt ID: Q8NBR6 (241-504) Ubiquitin carboxyl-terminal hydrolase C266A mutant

UniProt ID: P0CG48 (1-76) Polyubiquitin-C
Ubiquitin carboxyl-terminal hydrolase C266A mutantPolyubiquitin-C experimental SAS data
CUSTOM IN-HOUSE model
Sample: Ubiquitin carboxyl-terminal hydrolase C266A mutant monomer, 31 kDa Homo sapiens protein
Polyubiquitin-C pentamer, 43 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 May 26
Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2. Mol Cell (2021)
Abdul Rehman SA, Armstrong LA, Lange SM, Kristariyanto YA, Gräwert TW, Knebel A, Svergun DI, Kulathu Y
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 116 nm3

SASDJF3 – Aldo-keto reductase family 1 member B1 (AKR1B1) in the presence of 100 mM 5-methyl uridine

UniProt ID: P15121 (1-316) Aldo-keto reductase family 1 member B1
Aldo-keto reductase family 1 member B1 experimental SAS data
Aldo-keto reductase family 1 member B1 Kratky plot
Sample: Aldo-keto reductase family 1 member B1 monomer, 36 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 100 mM 5-methyl uridine, pH: 8
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2019 Jun 14
Improving data quality and expanding BioSAXS experiments to low-molecular-weight and low-concentration protein samples. Acta Crystallogr D Struct Biol 76(Pt 10):971-981 (2020)
Castellví A, Pascual-Izarra C, Crosas E, Malfois M, Juanhuix J
RgGuinier 2.0 nm
Dmax 6.5 nm
VolumePorod 52 nm3

SASDJG3 – Bovine Liver Catalase in presence of 100 mM 5-methyl uridine

UniProt ID: P00432 (1-527) Catalase
Catalase experimental SAS data
Catalase Kratky plot
Sample: Catalase tetramer, 240 kDa Bos taurus protein
Buffer: 50 mM sodium phosphate, pH: 7
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2019 Jun 14
Improving data quality and expanding BioSAXS experiments to low-molecular-weight and low-concentration protein samples. Acta Crystallogr D Struct Biol 76(Pt 10):971-981 (2020)
Castellví A, Pascual-Izarra C, Crosas E, Malfois M, Juanhuix J
RgGuinier 3.7 nm
Dmax 11.5 nm
VolumePorod 265 nm3

SASDJH3 – Hen Egg White Lysozyme in presence of 100 mM 5-methyl uridine

UniProt ID: P00698 (1-147) Lysozyme C
Lysozyme C experimental SAS data
Lysozyme C Kratky plot
Sample: Lysozyme C monomer, 16 kDa Gallus gallus protein
Buffer: 40 mM sodium acetate, 150 mM NaCl, 100 mM 5-methyl uridine, pH: 3.8
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2019 Jun 7
Improving data quality and expanding BioSAXS experiments to low-molecular-weight and low-concentration protein samples. Acta Crystallogr D Struct Biol 76(Pt 10):971-981 (2020)
Castellví A, Pascual-Izarra C, Crosas E, Malfois M, Juanhuix J
RgGuinier 1.5 nm
Dmax 4.2 nm
VolumePorod 21 nm3

SASDJJ3 – SH3 domain of alpha spectrin (amino acids 965-1025) in presence of 100 mM 5-methyl uridine

UniProt ID: P07751 (965-1025) Spectrin alpha chain, non-erythrocytic 1
Spectrin alpha chain, non-erythrocytic 1 experimental SAS data
Spectrin alpha chain, non-erythrocytic 1 Kratky plot
Sample: Spectrin alpha chain, non-erythrocytic 1, 7 kDa Gallus gallus protein
Buffer: 10 mM citric acid, 150 mM NaCl, 100 mM 5-methyl uridine, pH: 3
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2019 Jun 14
Improving data quality and expanding BioSAXS experiments to low-molecular-weight and low-concentration protein samples. Acta Crystallogr D Struct Biol 76(Pt 10):971-981 (2020)
Castellví A, Pascual-Izarra C, Crosas E, Malfois M, Juanhuix J
RgGuinier 1.3 nm
Dmax 4.5 nm
VolumePorod 10 nm3

SASDJK3 – Native alpha-2-macroglobulin, glycosylated

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Alpha-2-macroglobulin experimental SAS data
OTHER model
Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 7.7 nm
Dmax 22.7 nm

SASDJL3 – Methylamine-treated alpha-2-macroglobulin, glycosylated

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Alpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 6.7 nm
Dmax 19.7 nm

SASDJM3 – Trypsin-treated alpha-2-macroglobulin, glycosylated

UniProt ID: P00760 (1-246) Cationic trypsin

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Cationic trypsinAlpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Cationic trypsin dimer, 52 kDa Bos taurus protein
Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 15
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 19.7 nm