Browse by MODEL: No model

SASDMY5 – Truncated Zea mays beta-amylase (ZmBAM7) short

Beta-amylase experimental SAS data
Beta-amylase Kratky plot
Sample: Beta-amylase tetramer, 231 kDa Zea mays protein
Buffer: 50 mM HEPES, 25 mM NaCl, and 0.2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7
The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2 Acta Crystallographica Section D Structural Biology 78(5) (2022)
Ravenburg C, Riney M, Monroe J, Berndsen C
RgGuinier 5.1 nm
Dmax 13.9 nm
VolumePorod 467 nm3

SASDM26 – Sweet potato beta-amylase 5

Beta-amylase experimental SAS data
Beta-amylase Kratky plot
Sample: Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer: 20 mM HEPES, 150 mM NaCl, and 0.2 mM TCEP, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7
The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2 Acta Crystallographica Section D Structural Biology 78(5) (2022)
Ravenburg C, Riney M, Monroe J, Berndsen C
RgGuinier 4.4 nm
Dmax 14.1 nm
VolumePorod 296 nm3

SASDKK3 – SEC-SAXS of Presequence Protease (PreP)

Presequence protease, mitochondrial experimental SAS data
Presequence protease, mitochondrial Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 4
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.2 nm
Dmax 9.1 nm
VolumePorod 170 nm3

SASDKL3 – SEC-SAXS of Presequence Protease (PreP) with inhibitor MitoBloCK-60 (MB-60)

Presequence protease, mitochondrial experimental SAS data
Presequence protease, mitochondrial Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 7
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.1 nm
Dmax 9.1 nm
VolumePorod 165 nm3

SASDKM3 – SEC-SAXS of Presequence Protease (PreP) with pre-sequence of citrate synthase (1-27)

Presequence protease, mitochondrialCitrate synthase, mitochondrial experimental SAS data
Presequence protease, mitochondrial Citrate synthase, mitochondrial Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Citrate synthase, mitochondrial monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl , 20 mM EDTA, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Nov 4
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.1 nm
Dmax 8.7 nm
VolumePorod 165 nm3

SASDKN3 – SEC-SAXS of Presequence Protease (PreP) with Amyloid beta precursor protein (1-40)

Presequence protease, mitochondrialAmyloid-beta precursor protein experimental SAS data
Presequence protease, mitochondrial Amyloid-beta precursor protein Kratky plot
Sample: Presequence protease, mitochondrial monomer, 115 kDa Homo sapiens protein
Amyloid-beta precursor protein monomer, 4 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl , 20 mM EDTA, pH: 7.7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Mar 7
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition Nature Communications 13(1) (2022)
Liang W, Wijaya J, Wei H, Noble A, Mancl J, Mo S, Lee D, Lin King J, Pan M, Liu C, Koehler C, Zhao M, Potter C, Carragher B, Li S, Tang W
RgGuinier 3.0 nm
Dmax 8.5 nm
VolumePorod 175 nm3

SASDN22 – Dockerin domain-containing protein, starch adherence system 20 (Sas20), domain 1 with maltoheptaose

Dockerin domain-containing protein experimental SAS data
Dockerin domain-containing protein Kratky plot
Sample: Dockerin domain-containing protein monomer, 26 kDa Ruminococcus bromii protein
Buffer: phosphate buffered saline, 1 mM TCEP, pH: 7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 14
Sas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome Journal of Biological Chemistry :101896 (2022)
Cerqueira F, Photenhauer A, Doden H, Brown A, Abdel-Hamid A, Moraïs S, Bayer E, Wawrzak Z, Cann I, Ridlon J, Hopkins J, Koropatkin N
RgGuinier 2.0 nm
Dmax 7.8 nm
VolumePorod 45 nm3

SASDN42 – Dockerin domain-containing protein, starch adherence system 20 (Sas20), domains 1 and 2 with maltoheptaose

Dockerin domain-containing protein experimental SAS data
Dockerin domain-containing protein Kratky plot
Sample: Dockerin domain-containing protein monomer, 26 kDa Ruminococcus bromii protein
Buffer: phosphate buffered saline, 1 mM TCEP, pH: 7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 14
Sas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome Journal of Biological Chemistry :101896 (2022)
Cerqueira F, Photenhauer A, Doden H, Brown A, Abdel-Hamid A, Moraïs S, Bayer E, Wawrzak Z, Cann I, Ridlon J, Hopkins J, Koropatkin N
RgGuinier 5.2 nm
Dmax 19.0 nm
VolumePorod 84 nm3

SASDNW5 – apo Roquin-1 (coreROQ) at 50 µM, including concentration series data at 100, 200, 300 µM

Roquin-1 experimental SAS data
Roquin-1 Kratky plot
Sample: Roquin-1 monomer, 18 kDa Mus musculus protein
Buffer: 150 mM NaCl, 20 mM Tris, 2 mM TCEP, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 1
NMR-derived secondary structure of the full-length Ox40 mRNA 3'UTR and its multivalent binding to the immunoregulatory RBP Roquin. Nucleic Acids Res (2022)
Tants JN, Becker LM, McNicoll F, Müller-McNicoll M, Schlundt A
RgGuinier 1.9 nm
Dmax 7.0 nm
VolumePorod 35 nm3

SASDNX5 – apo Roquin-1 (extROQ) at 50 µM, including concentration series data at 100, 200, 300 µM

Roquin-1 extROQ experimental SAS data
Roquin-1 extROQ Kratky plot
Sample: Roquin-1 extROQ monomer, 35 kDa Mus musculus protein
Buffer: 150 mM NaCl, 20 mM Tris, 2 mM TCEP, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 1
NMR-derived secondary structure of the full-length Ox40 mRNA 3'UTR and its multivalent binding to the immunoregulatory RBP Roquin. Nucleic Acids Res (2022)
Tants JN, Becker LM, McNicoll F, Müller-McNicoll M, Schlundt A
RgGuinier 2.8 nm
Dmax 14.0 nm
VolumePorod 53 nm3