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15 hits found for Beta-amylase

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

SASDA62 – bAmylase in PBS

Beta-amylase experimental SAS data
DAMMIF model
Sample: Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 20
Standard proteins
Darja Ruskule
RgGuinier 4.2 nm
Dmax 12.7 nm
VolumePorod 214 nm3

SASDWB4 – ...beta-amylase from AF4-SAXS measurement

Beta-amylase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer: phosphate buffered saline, 1% glycerol, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 13
AF4-to-SAXS: expanded characterization of nanoparticles and proteins at the P12 BioSAXS beamline. J Synchrotron Radiat (2025)
Da Vela S, Bartels K, Franke D, Soloviov D, Gräwert T, Molodenskiy D, Kolb B, Wilhelmy C, Drexel R, Meier F, Haas H, Langguth P, Graewert MA
RgGuinier 4.2 nm
Dmax 12.6 nm
VolumePorod 297 nm3

SASDGY4 – Beta-amylase 2, chloroplastic (AtBAM2)

Beta-amylase 2, chloroplastic experimental SAS data
YASARA model
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
Solution structure and assembly of β-amylase2 from Arabidopsis thaliana (2019)
Chandrasekharan N, Ravenburg C, Roy I, Monroe J, Berndsen C
RgGuinier 4.2 nm
Dmax 12.6 nm
VolumePorod 308 nm3

SASDGZ4 – Beta-amylase 2, chloroplastic (AtBAM2) Ndel1

Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 215 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
Solution structure and assembly of β-amylase2 from Arabidopsis thaliana (2019)
Chandrasekharan N, Ravenburg C, Roy I, Monroe J, Berndsen C
RgGuinier 4.4 nm
Dmax 11.0 nm
VolumePorod 272 nm3

SASDMX5 – ...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 5.3 nm
Dmax 16.3 nm
VolumePorod 615 nm3

SASDVX5 – pseudoamylase BAM9

Inactive beta-amylase 9 experimental SAS data
ALPHAFOLD model
Sample: ...beta-amylase 9 monomer, 50 kDa Arabidopsis thaliana protein
Buffer: 20 mM HEPES, 100 mM NaCl, 0.2 mM TCEP, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 May 16
The Pseudoenzyme β‐Amylase9 From Arabidopsis Activates α‐Amylase3: A Possible Mechanism to Promote Stress‐Induced Starch Degradation Proteins: Structure, Function, and Bioinformatics (2025)
Berndsen C, Storm A, Sardelli A, Hossain S, Clermont K, McFather L, Connor M, Monroe J
RgGuinier 2.4 nm
Dmax 8.7 nm
VolumePorod 87 nm3

SASDMY5 – ...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

SASDVY5 – pseudoamylase BAM9 bound to alpha-amylase AMY3

Inactive beta-amylase 9Alpha-amylase 3, chloroplastic experimental SAS data
BILBOMD model
Sample: ...beta-amylase 9 monomer, 50 kDa Arabidopsis thaliana protein
Alpha-amylase 3, chloroplastic monomer, 94 kDa Arabidopsis thaliana protein
Buffer: 20 mM HEPES, 100 mM NaCl, 0.2 mM TCEP, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 May 16
The Pseudoenzyme β‐Amylase9 From Arabidopsis Activates α‐Amylase3: A Possible Mechanism to Promote Stress‐Induced Starch Degradation Proteins: Structure, Function, and Bioinformatics (2025)
Berndsen C, Storm A, Sardelli A, Hossain S, Clermont K, McFather L, Connor M, Monroe J
RgGuinier 5.0 nm
Dmax 25.5 nm
VolumePorod 380 nm3

SASDMZ5 – ...beta-amylase 1

Beta-amylase 1, chloroplastic experimental SAS data
YASARA model
Sample: Beta-amylase 1, chloroplastic monomer, 65 kDa Arabidopsis thaliana protein
Buffer: 50 mM MES, 100 mM NaCl, 1 mM DTT, pH: 6.7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 22
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 2.6 nm
Dmax 9.8 nm
VolumePorod 88 nm3

SASDM26 – ...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

SASDCE8 – Beta amylase from sweet potato (WAXS)

Beta-amylase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer: tbs, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jul 15
WAXS benchmark on standard proteins
Maxim Petoukhov
RgGuinier 4.0 nm

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