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SASDTP2 – Ubiquitin carboxy-terminal hydrolase L1 (UCHL1) wild type

Ubiquitin carboxyl-terminal hydrolase isozyme L1 experimental SAS data
Ubiquitin carboxyl-terminal hydrolase isozyme L1 Kratky plot
Sample: Ubiquitin carboxyl-terminal hydrolase isozyme L1 monomer, 26 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM TCEP, 0.03% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 Sep 2
Altered protein dynamics and a more reactive catalytic cysteine in a neurodegeneration-associated UCHL1 mutant. J Mol Biol :168438 (2024)
Kenny S, Lai CH, Chiang TS, Brown K, Hewitt CS, Krabill AD, Chang HT, Wang YS, Flaherty DP, Danny Hsu ST, Das C
RgGuinier 1.9 nm
Dmax 5.9 nm
VolumePorod 26 nm3

SASDTQ2 – Ubiquitin carboxy-terminal hydrolase L1 (UCHL1) R178Q mutant

Ubiquitin carboxyl-terminal hydrolase isozyme L1 (R178Q) experimental SAS data
Ubiquitin carboxyl-terminal hydrolase isozyme L1 (R178Q) Kratky plot
Sample: Ubiquitin carboxyl-terminal hydrolase isozyme L1 (R178Q) monomer, 26 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM TCEP, 0.03% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 Sep 2
Altered protein dynamics and a more reactive catalytic cysteine in a neurodegeneration-associated UCHL1 mutant. J Mol Biol :168438 (2024)
Kenny S, Lai CH, Chiang TS, Brown K, Hewitt CS, Krabill AD, Chang HT, Wang YS, Flaherty DP, Danny Hsu ST, Das C
RgGuinier 1.9 nm
Dmax 5.8 nm
VolumePorod 25 nm3

SASDTW2 – Protein phosphatase 2A (PP2A)-B56δ holoenzyme wildtype

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformIsoform Delta-1 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (R160H)Isoform 1 of Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform experimental SAS data
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform Isoform Delta-1 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (R160H) Isoform 1 of Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform Kratky plot
Sample: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform monomer, 65 kDa Homo sapiens protein
Isoform Delta-1 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (R160H) monomer, 70 kDa Homo sapiens protein
Isoform 1 of Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform monomer, 36 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 50 µM MnCl2, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Nov 20
B56δ long-disordered arms form a dynamic PP2A regulation interface coupled with global allostery and Jordan's syndrome mutations. Proc Natl Acad Sci U S A 121(1):e2310727120 (2024)
Wu CG, Balakrishnan VK, Merrill RA, Parihar PS, Konovolov K, Chen YC, Xu Z, Wei H, Sundaresan R, Cui Q, Wadzinski BE, Swingle MR, Musiyenko A, Chung WK, Honkanen RE, Suzuki A, Huang X, Strack S, Xing Y
RgGuinier 4.0 nm
Dmax 12.0 nm
VolumePorod 266 nm3

SASDTX2 – Protein phosphatase 2A (PP2A)-B56δ holoenzyme E198K mutant

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformIsoform 1 of Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformIsoform Delta-1 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (R160H, E198K) experimental SAS data
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform Isoform 1 of Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform Isoform Delta-1 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (R160H, E198K) Kratky plot
Sample: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform monomer, 65 kDa Homo sapiens protein
Isoform 1 of Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform monomer, 36 kDa Homo sapiens protein
Isoform Delta-1 of Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (R160H, E198K) monomer, 70 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 50 µM MnCl2, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Nov 20
B56δ long-disordered arms form a dynamic PP2A regulation interface coupled with global allostery and Jordan's syndrome mutations. Proc Natl Acad Sci U S A 121(1):e2310727120 (2024)
Wu CG, Balakrishnan VK, Merrill RA, Parihar PS, Konovolov K, Chen YC, Xu Z, Wei H, Sundaresan R, Cui Q, Wadzinski BE, Swingle MR, Musiyenko A, Chung WK, Honkanen RE, Suzuki A, Huang X, Strack S, Xing Y
RgGuinier 4.2 nm
Dmax 14.0 nm
VolumePorod 305 nm3

SASDTG2 – LCP domain of LytR from Streptococcus dysgalactiae in the presence of geranylgeranyl diphosphate (150 mM NaCl)

Biofilm regulatory protein experimental SAS data
Biofilm regulatory protein Kratky plot
Sample: Biofilm regulatory protein monomer, 34 kDa Streptococcus dysgalactiae subsp. … protein
Buffer: 50 mM HEPES, 150 mM NaCl, 5 mM MgCl2, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2022 Jun 1
Structural insights of an LCP protein-LytR-from Streptococcus dysgalactiae subs. dysgalactiae through biophysical and in silico methods. Front Chem 12:1379914 (2024)
Paquete-Ferreira J, Freire F, Fernandes HS, Muthukumaran J, Ramos J, Bryton J, Panjkovich A, Svergun D, Santos MFA, Correia MAS, Fernandes AR, Romão MJ, Sousa SF, Santos-Silva T
RgGuinier 2.5 nm
Dmax 8.0 nm
VolumePorod 83 nm3

SASDTH2 – LCP domain of LytR from Streptococcus dysgalactiae in the absence of ligand (150 mM NaCl)

Biofilm regulatory protein experimental SAS data
Biofilm regulatory protein Kratky plot
Sample: Biofilm regulatory protein monomer, 34 kDa Streptococcus dysgalactiae subsp. … protein
Buffer: 50 mM HEPES, 150 mM NaCl, 5 mM MgCl2, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2022 Jun 1
Structural insights of an LCP protein-LytR-from Streptococcus dysgalactiae subs. dysgalactiae through biophysical and in silico methods. Front Chem 12:1379914 (2024)
Paquete-Ferreira J, Freire F, Fernandes HS, Muthukumaran J, Ramos J, Bryton J, Panjkovich A, Svergun D, Santos MFA, Correia MAS, Fernandes AR, Romão MJ, Sousa SF, Santos-Silva T
RgGuinier 2.4 nm
Dmax 9.0 nm
VolumePorod 76 nm3

SASDUY9 – BAM2 in 100 mM KCl (0.25 mg/mL)

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 17
Potassium cations expand the conformation ensemble of Arabidopsis thaliana β-amylase2 (BAM2). MicroPubl Biol 2024 (2024)
Sholes A, Asongakap R, Jaconski S, Monroe J, Berndsen CE
RgGuinier 4.9 nm
Dmax 16.4 nm
VolumePorod 226 nm3

SASDUZ9 – BAM2 in 100 mM KCl (0.5 mg/mL)

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 17
Potassium cations expand the conformation ensemble of Arabidopsis thaliana β-amylase2 (BAM2). MicroPubl Biol 2024 (2024)
Sholes A, Asongakap R, Jaconski S, Monroe J, Berndsen CE
RgGuinier 4.9 nm
Dmax 15.0 nm
VolumePorod 234 nm3

SASDV22 – BAM2 in 100 mM KCl (1 mg/mL)

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 17
Potassium cations expand the conformation ensemble of Arabidopsis thaliana β-amylase2 (BAM2). MicroPubl Biol 2024 (2024)
Sholes A, Asongakap R, Jaconski S, Monroe J, Berndsen CE
RgGuinier 4.7 nm
Dmax 15.1 nm
VolumePorod 218 nm3

SASDV32 – BAM2 in 100 mM KCl (2 mg/mL)

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 17
Potassium cations expand the conformation ensemble of Arabidopsis thaliana β-amylase2 (BAM2). MicroPubl Biol 2024 (2024)
Sholes A, Asongakap R, Jaconski S, Monroe J, Berndsen CE
RgGuinier 4.7 nm
Dmax 15.0 nm
VolumePorod 220 nm3